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Showing drug card for 4-Androstenedione (DB01536)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-02-19 16:04:39
Primary Accession Number DB01536
Secondary Accession Number
  • EXPT00569
Name 4-Androstenedione
Drug Type
  • Experimental
  • Illicit
  • Small Molecule
Description A delta-4 C19 steroid that is produced not only in the testis, but also in the ovary and the adrenal cortex. Depending on the tissue type, androstenedione can serve as a precursor to testosterone as well as estrone and estradiol. [PubChem]
Synonyms Not Available
Brand Names Not Available
Brand Mixtures Not Available
Chemical IUPAC Name (8R,9S,10R,13S,14S)-10,13-dimethyl-2,6,7,8,9,11,12,14,15,16-decahydro-1H-cyclopenta[a]phenanthrene-3,17-dione
Chemical Formula C19H26O2
Chemical Structure Structure
CAS Registry Number 63-05-8
InChI Identifier InChI=1/C19H26O2/c1-18-9-7-13(20)11-12(18)3-4-14-15-5-6-17(21)19(15,2)10-8-16(14)18/h11,14-16H,3-10H2,1-2H3/t14-,15-,16-,18-,19-/m0/s1
InChI Key AEMFNILZOJDQLW-QAGGRKNEBJ
KEGG Drug D00051 Link Image
KEGG Compound C00280 Link Image
PubChem Compound 6128 Link Image
PubChem Substance 3575 Link Image
ChEBI ID 16422 Link Image
PharmGKB ID Not Available
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] Not Available
RxList Link Not Available
PDRhealth Link Not Available
Wikipedia Link Not Available
FDA Label Not Available
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference Not Available
Average Molecular Weight 286.4085
Monoisotopic Molecular Weight 286.1933
State Solid
Melting Point Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 2.70e-02 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP 2.93 Calculated using ALOGPS
Experimental LogS -3.69 [ADME Research, USCD]
Predicted LogS -4.03 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point Not Available
Mass Spectrum Not Available
MOL File Show Link Image | Download Link Image
SDF File Show Link Image | Download Link Image
PDB File Show Link Image | Download Link Image
2D Structure
3D Structure
Experimental PDB ID 1XF0 Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES C[C@]12CC[C@H]3[C@@H](CCC4=CC(=O)CC[C@]34C)[C@@H]1CCC2=O
Canonical SMILES CC12CCC3C(CCC4=CC(=O)CCC34C)C1CCC2=O
Drug Category Not Available
ATC Codes Not Available
AHFS Codes Not Available
Indication Not Available
Pharmacology Not Available
Mechanism of Action Not Available
Absorption Not Available
Toxicity Not Available
Protein Binding Not Available
Biotransformation Not Available
Half Life Not Available
Dosage Forms Not Available
Patient Information Not Available
Contraindications Not Available
Interactions Not Available
Drug Interactions Not Available
Food Interactions Not Available
Pathways Not Available
General References Not Available
Organisms Affected Not Available
Targets
  1. Estradiol 17-beta-dehydrogenase 1
  2. Aldo-keto reductase family 1 member C3
  3. 6-deoxyerythronolide B hydroxylase
Drug Target 1 [top]
Target 1 ID 217
Target 1 Name Estradiol 17-beta-dehydrogenase 1
Target 1 Synonyms
  1. 17-beta- hydroxysteroid dehydrogenase type 1
  2. 17-beta-HSD 1
  3. 20 alpha-hydroxysteroid dehydrogenase
  4. 20-alpha-HSD
  5. E2DH
  6. EC 1.1.1.62
  7. Placental 17- beta-hydroxysteroid dehydrogenase
Target 1 Gene Name HSD17B1
Target 1 Protein Sequence >Estradiol 17-beta-dehydrogenase 1 
ARTVVLITGCSSGIGLHLAVRLASDPSQSFKVYATLRDLKTQGRLWEAARALACPPGSLE
TLQLDVRDSKSVAAARERVTEGRVDVLVCNAGLGLLGPLEALGEDAVASVLDVNVVGTVR
MLQAFLPDMKRRGSGRVLVTGSVGGLMGLPFNDVYCASKFALEGLCESLAVLLLPFGVHL
SLIECGPVHTAFMEKVLGSPEEVLDRTDIHTFHRFYQYLAHSKQVFREAAQNPEEVAEVF
LTALRAPKPTLRYFTTERFLPLLRMRLDDPSGSNYVTAMHREVFGDVPAKAEAGAEAGGG
AGPGAEDEAGRSAVGDPELGDPPAAPQ
Target 1 Number of Residues 332
Target 1 Molecular Weight 34849
Target 1 Theoretical pI 5.42
Target 1 GO Classification
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on CH-OH group of donors
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
steroid dehydrogenase activity
estradiol 17-beta-dehydrogenase activity
Process
physiological process
metabolism
primary metabolism
lipid metabolism
cellular lipid metabolism
steroid metabolism
steroid biosynthesis
estrogen biosynthesis
Component
cell
intracellular
cytoplasm
Target 1 General Function Lipid transport and metabolism
Target 1 Specific Function Favors the reduction of estrogens and androgens. Also has 20-alpha-HSD activity. Uses preferentially NADH
Target 1 Pathways
Name SMPDB Link KEGG Link
Androgen and estrogen metabolism SMP00068 Link Image map00150 Link Image
Target 1 Reactions
  • estradiol-17beta + NAD(P)+ = estrone + NAD(P)H + H+
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 23365 Link Image
Target 1 UniProtKB/Swiss-Prot ID P14061 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name DHB1_HUMAN Link Image
Target 1 PDB ID 1QYX Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • Cytoplasm
Target 1 Gene Sequence >987 bp 
ATGGCCCGCACCGTGGTGCTCATCACCGGCTGTTCCTCGGGCATCGGCCTGCACTTGGCC
GTACGTCTGGCTTCAGATCCATCCCAGAGCTTCAAAGTGTATGCCACGTTGAGGGACCTG
AAAACACAGGGCCGGCTGTGGGAGGCGGCCCGGGCCCTGGCATGCCCTCCGGGATCCCTG
GAGACGTTGCAGCTGGACGTAAGGGACTCAAAATCCGTGGCCGCTGCCCGGGAACGCGTG
ACTGAGGGCCGCGTGGACGTGCTGGTGTGTAACGCAGGCCTGGGCCTGCTGGGGCCGCTG
GAGGCGCTGGGGGAGGACGCCGTGGCCTCTGTGCTGGACGTGAATGTAGTAGGGACTGTG
CGGATGCTGCAGGCCTTCCTGCCAGACATGAAGAGGCGCGGTTCGGGACGCGTGTTGGTG
ACCGGGAGCGTGGGAGGATTGATGGGGCTGCCTTTCAATGACGTTTATTGCGCCAGCAAG
TTCGCGCTCGAAGGCTTATGCGAGAGTCTGGCGGTTCTGCTGCTGCCCTTTGGGGTCCAC
TTGAGCCTGATCGAGTGCGGCCCAGTGCACACCGCCTTCATGGAGAAGGTGTTGGGCAGC
CCAGAGGAGGTGCTGGACCGCACGGACATCCACACCTTCCACCGCTTCTACCAATACCTC
GCCCACAGCAAGCAAGTCTTTCGCGAGGCGGCGCAGAACCCTGAGGAGGTGGCGGAGGTC
TTCCTCACCGCTTTGCGCGCCCCGAAGCCGACCCTGCGCTACTTCACCACCGAGCGCTTC
CTGCCCCTGCTGCGGATGCGCCTGGACGACCCCAGCGGCTCCAACTACGTCACCGCCATG
CACCGGGAAGTGTTCGGCGACGTTCCGGCAAAGGCCGAGGCTGGGGCCGAGGCTGGGGGC
GGGGCCGGGCCTGGGGCAGAGGACGAGGCCGGGCGCAGTGCGGTGGGGGACCCTGAGCTC
GGCGATCCTCCGGCCGCCCCGCAGTAA
Target 1 GenBank Gene ID
Target 1 GeneCard ID HSD17B1 Link Image
Target 1 GenAtlas ID HSD17B1 Link Image
Target 1 HGNC ID HGNC:5210 Link Image
Target 1 Chromosome Location 17
Target 1 Locus 17q11-q21
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Han Q, Campbell RL, Gangloff A, Huang YW, Lin SX: Dehydroepiandrosterone and dihydrotestosterone recognition by human estrogenic 17beta-hydroxysteroid dehydrogenase. C-18/c-19 steroid discrimination and enzyme-induced strain. J Biol Chem. 2000 Jan 14;275(2):1105-11. [PubMed Link Image]
  2. Peltoketo H, Isomaa V, Vihko R: Genomic organization and DNA sequences of human 17 beta-hydroxysteroid dehydrogenase genes and flanking regions. Localization of multiple Alu sequences and putative cis-acting elements. Eur J Biochem. 1992 Oct 1;209(1):459-66. [PubMed Link Image]
  3. Luu-The V, Labrie C, Zhao HF, Couet J, Lachance Y, Simard J, Cote J, Leblanc G, Lagace L, Berube D, et al.: Purification, cloning, complementary DNA structure, and predicted amino acid sequence of human estradiol 17 beta-dehydrogenase. Ann N Y Acad Sci. 1990;595:40-52. [PubMed Link Image]
  4. Luu-The V, Labrie C, Simard J, Lachance Y, Zhao HF, Couet J, Leblanc G, Labrie F: Structure of two in tandem human 17 beta-hydroxysteroid dehydrogenase genes. Mol Endocrinol. 1990 Feb;4(2):268-75. [PubMed Link Image]
  5. Baker ME: Human placental 17 beta-hydroxysteroid dehydrogenase is homologous to NodG protein of Rhizobium meliloti. Mol Endocrinol. 1989 May;3(5):881-4. [PubMed Link Image]
  6. Luu The V, Labrie C, Zhao HF, Couet J, Lachance Y, Simard J, Leblanc G, Cote J, Berube D, Gagne R, et al.: Characterization of cDNAs for human estradiol 17 beta-dehydrogenase and assignment of the gene to chromosome 17: evidence of two mRNA species with distinct 5'-termini in human placenta. Mol Endocrinol. 1989 Aug;3(8):1301-9. [PubMed Link Image]
  7. Peltoketo H, Isomaa V, Maentausta O, Vihko R: Complete amino acid sequence of human placental 17 beta-hydroxysteroid dehydrogenase deduced from cDNA. FEBS Lett. 1988 Oct 24;239(1):73-7. [PubMed Link Image]
  8. Galdes A, Auld DS, Vallee BL: Elucidation of the chemical nature of the steady-state intermediates in the mechanism of carboxypeptidase A. Biochemistry. 1986 Feb 11;25(3):646-51. [PubMed Link Image]
  9. Nicolas JC, Harris JI: Human placental 17 -oestradiol dehydrogenase. Sequence of a tryptic peptide containing an essential cysteine. FEBS Lett. 1973 Jan 15;29(2):173-6. [PubMed Link Image]
  10. Burns DJ, Engel LL, Bethune JL: Amino acid composition and subunit structure. Human placental 17 -estradiol dehydrogenase. Biochemistry. 1972 Jul 4;11(14):2699-703. [PubMed Link Image]
  11. 6578212 Murdock GL, Chin CC, Offord RE, Bradshaw RA, Warren JC: Human placental estradiol 17 beta-dehydrogenase. Identification of a single histidine residue affinity-labeled by both 3-bromoacetoxyestrone and 12 beta-bromoacetoxy-4-estrene-3,17-dione. J Biol Chem. 1983 Oct 10;258(19):11460-4.
  12. 7663947 Ghosh D, Pletnev VZ, Zhu DW, Wawrzak Z, Duax WL, Pangborn W, Labrie F, Lin SX: Structure of human estrogenic 17 beta-hydroxysteroid dehydrogenase at 2.20 A resolution. Structure. 1995 May 15;3(5):503-13.
  13. 8389226 Normand T, Narod S, Labrie F, Simard J: Detection of polymorphisms in the estradiol 17 beta-hydroxysteroid dehydrogenase II gene at the EDH17B2 locus on 17q11-q21. Hum Mol Genet. 1993 Apr;2(4):479-83.
  14. 8805577 Breton R, Housset D, Mazza C, Fontecilla-Camps JC: The structure of a complex of human 17beta-hydroxysteroid dehydrogenase with estradiol and NADP+ identifies two principal targets for the design of inhibitors. Structure. 1996 Aug 15;4(8):905-15.
  15. 9525918 Mazza C, Breton R, Housset D, Fontecilla-Camps JC: Unusual charge stabilization of NADP+ in 17beta-hydroxysteroid dehydrogenase. J Biol Chem. 1998 Apr 3;273(14):8145-52.
Target 1 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 650
Target 2 Name Aldo-keto reductase family 1 member C3
Target 2 Synonyms
  1. 17-beta-HSD 5
  2. 17-beta-hydroxysteroid dehydrogenase type 5
  3. 3-alpha- hydroxysteroid dehydrogenase type 2
  4. 3-alpha-HSD type 2
  5. 3-alpha-HSD type II, brain
  6. Chlordecone reductase homolog HAKRb
  7. DD-3
  8. DD3
  9. Dihydrodiol dehydrogenase 3
  10. Dihydrodiol dehydrogenase type I
  11. EC 1.-.-.-
  12. EC 1.1.1.188
  13. EC 1.1.1.213
  14. EC 1.1.1.62
  15. EC 1.3.1.20
  16. Estradiol 17-beta-dehydrogenase
  17. HA1753
  18. PGFS
  19. Prostaglandin F synthase
  20. Trans-1,2- dihydrobenzene-1,2-diol dehydrogenase
Target 2 Gene Name AKR1C3
Target 2 Protein Sequence >Aldo-keto reductase family 1 member C3 
MDSKQQCVKLNDGHFMPVLGFGTYAPPEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQ
VGLAIRSKIADGSVKREDIFYTSKLWSTFHRPELVRPALENSLKKAQLDYVDLYLIHSPM
SLKPGEELSPTDENGKVIFDIVDLCTTWEAMEKCKDAGLAKSIGVSNFNRRQLEMILNKP
GLKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRDKRWVDPNSPVLLEDPV
LCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLD
RNLHYFNSDSFASHPNYPYSDEY
Target 2 Number of Residues 328
Target 2 Molecular Weight 36845
Target 2 Theoretical pI 8.06
Target 2 GO Classification
Function
catalytic activity
oxidoreductase activity
Process
Not Available
Component
Not Available
Target 2 General Function Involved in oxidoreductase activity
Target 2 Specific Function Catalyzes the conversion of aldehydes and ketones to alcohols. Catalyzes the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ) and the oxidation of 9alpha,11beta- PGF2 to PGD2. Functions as a bi-directional 3alpha-, 17beta- and 20alpha HSD. Can interconvert active androgens, estrogens and progestins with their cognate inactive metabolites. Preferentially transforms androstenedione (4-dione) to testosterone
Target 2 Pathways
Name SMPDB Link KEGG Link
Prostaglandin and leukotriene metabolism map00590 Link Image
Target 2 Reactions
  • estradiol-17beta + NAD(P)+ = estrone + NAD(P)H + H+
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 4261711 Link Image
Target 2 UniProtKB/Swiss-Prot ID P42330 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name AK1C3_HUMAN Link Image
Target 2 PDB ID 1XF0 Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location
  • Cytoplasm
Target 2 Gene Sequence >972 bp 
ATGGATTCCAAACAGCAGTGTGTAAAGCTAAATGATGGCCACTTCATGCCTGTATTGGGA
TTTGGCACCTATGCACCTCCAGAGGTTCCGAGAAGTAAAGCTTTGGAGGTCACAAAATTA
GCAATAGAAGCTGGGTTCCGCCATATAGATTCTGCTCATTTATACAATAATGAGGAGCAG
GTTGGACTGGCCATCCGAAGCAAGATTGCAGATGGCAGTGTTGAGAGAGAAGACATATTC
TACACTTCAAAGCTTTGGTCCACTTTTCATCGACCAGAGTTGGTCCGACCAGCCTTGGAA
AACTCACTGAAGAAAGCTCAATTGGACTATGTTGACCTCTATCTTATTCATTCTCCAATG
TCTCTAAAGCCAGGTGAGGAACTTTCACCAACAGATGAAAATGGAAAAGTAATATTTGAC
ATAGTGGATCTCTGTACCACCTGGGAGGCCATGGAGAAGTGTAAGGATGCAGGATTGGCC
AAGTCCATTGGGGTATCAAACTTCAACCGCAGGCAGCTGGAGATCATCCTCAACAAGCCA
GGACTCAAGTACAAGCCTGTCTGCAACCAGGTAGAATGTCATCCGTATTTCAACCGGAGT
AAATTGCTAGATTTCTGCAAGTCGAAAGATATTGTTCTGGTTGCCTATAGTGCTCTGGGA
TCTCAACGAGACAAACGATGGGTGGACCCGAACTCCCCGGTCCTCTTGGAGGACCCAGTC
CTTTGTGCCTTGGCAAAAAAGCACAAGCGAACCCCAGCCCTGATTGCCCTGCGCTACCAG
CTGCAGCGTGGGGTTGTGGTCCTGGCCAAGAGCTACAATGAGCAGCGCATCAGACAGAAC
GTGCAGGTTTTTGAGTTCCAGTTGACTGCAGAGGACATGAAAGCCATAGATGGCCTAGAC
AGAAATCTCCACTATTTTAACAGTGATAGTTTTGCTAGCCACCCTAATTATCCATATTCA
GATGAATATTAA
Target 2 GenBank Gene ID
Target 2 GeneCard ID AKR1C3 Link Image
Target 2 GenAtlas ID AKR1C3 Link Image
Target 2 HGNC ID HGNC:386 Link Image
Target 2 Chromosome Location 10
Target 2 Locus 10p15-p14
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Griffin LD, Mellon SH: Selective serotonin reuptake inhibitors directly alter activity of neurosteroidogenic enzymes. Proc Natl Acad Sci U S A. 1999 Nov 9;96(23):13512-7. [PubMed Link Image]
  2. Suzuki-Yamamoto T, Nishizawa M, Fukui M, Okuda-Ashitaka E, Nakajima T, Ito S, Watanabe K: cDNA cloning, expression and characterization of human prostaglandin F synthase. FEBS Lett. 1999 Dec 3;462(3):335-40. [PubMed Link Image]
  3. Nishizawa M, Nakajima T, Yasuda K, Kanzaki H, Sasaguri Y, Watanabe K, Ito S: Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes. Genes Cells. 2000 Feb;5(2):111-25. [PubMed Link Image]
  4. Penning TM, Burczynski ME, Jez JM, Lin HK, Ma H, Moore M, Ratnam K, Palackal N: Structure-function aspects and inhibitor design of type 5 17beta-hydroxysteroid dehydrogenase (AKR1C3). Mol Cell Endocrinol. 2001 Jan 22;171(1-2):137-49. [PubMed Link Image]
  5. Khanna M, Qin KN, Cheng KC: Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans. J Steroid Biochem Mol Biol. 1995 Jun;53(1-6):41-6. [PubMed Link Image]
  6. Khanna M, Qin KN, Wang RW, Cheng KC: Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases. J Biol Chem. 1995 Aug 25;270(34):20162-8. [PubMed Link Image]
  7. Nagase T, Miyajima N, Tanaka A, Sazuka T, Seki N, Sato S, Tabata S, Ishikawa K, Kawarabayasi Y, Kotani H, et al.: Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1995;2(1):37-43. [PubMed Link Image]
  8. Qin KN, New MI, Cheng KC: Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase. J Steroid Biochem Mol Biol. 1993 Dec;46(6):673-9. [PubMed Link Image]
  9. Lin HK, Jez JM, Schlegel BP, Peehl DM, Pachter JA, Penning TM: Expression and characterization of recombinant type 2 3 alpha-hydroxysteroid dehydrogenase (HSD) from human prostate: demonstration of bifunctional 3 alpha/17 beta-HSD activity and cellular distribution. Mol Endocrinol. 1997 Dec;11(13):1971-84. [PubMed Link Image]
  10. Dufort I, Rheault P, Huang XF, Soucy P, Luu-The V: Characteristics of a highly labile human type 5 17beta-hydroxysteroid dehydrogenase. Endocrinology. 1999 Feb;140(2):568-74. [PubMed Link Image]
Target 2 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 2972
Target 3 Name 6-deoxyerythronolide B hydroxylase
Target 3 Synonyms
  1. 6-DEB hydroxylase
  2. CYPCVIIA1
  3. Cytochrome P450 107A1
  4. EC 1.-.-.-
  5. Erythomycin A biosynthesis hydrolase
  6. P450eryF
Target 3 Gene Name eryF
Target 3 Protein Sequence >6-deoxyerythronolide B hydroxylase 
MTTVPDLESDSFHVDWYRTYAELRETAPVTPVRFLGQDAWLVTGYDEAKAALSDLRLSSD
PKKKYPGVEVEFPAYLGFPEDVRNYFATNMGTSDPPTHTRLRKLVSQEFTVRRVEAMRPR
VEQITAELLDEVGDSGVVDIVDRFAHPLPIKVICELLGVDEKYRGEFGRWSSEILVMDPE
RAEQRGQAAREVVNFILDLVERRRTEPGDDLLSALIRVQDDDDGRLSADELTSIALVLLL
AGFEASVSLIGIGTYLLLTHPDQLALVRRDPSALPNAVEEILRYIAPPETTTRFAAEEVE
IGGVAIPQYSTVLVANGAANRDPKQFPDPHRFDVTRDTRGHLSFGQGIHFCMGRPLAKLE
GEVALRALFGRFPALSLGIDADDVVWRRSLLLRGIDHLPVRLDG
Target 3 Number of Residues 410
Target 3 Molecular Weight 45100
Target 3 Theoretical pI 4.69
Target 3 GO Classification
Function
tetrapyrrole binding
heme binding
binding
ion binding
cation binding
transition metal ion binding
iron ion binding
catalytic activity
oxidoreductase activity
monooxygenase activity
Process
physiological process
metabolism
cellular metabolism
generation of precursor metabolites and energy
electron transport
Component
Not Available
Target 3 General Function Secondary metabolites biosynthesis, transport and catabolism
Target 3 Specific Function Conversion of 6-deoxyerythronolide B (6-DEB) to erythronolide B (EB) by the insertion of an oxygen at the 6S position of 6-DEB
Target 3 Pathways Not Available
Target 3 Reactions Not Available
Target 3 Pfam Domain Function
Target 3 Signals
  • None
Target 3 Transmembrane Regions
  • None
Target 3 Essentiality Essential
Target 3 GenBank ID Protein 48942 Link Image
Target 3 UniProtKB/Swiss-Prot ID Q00441 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name CPXJ_SACER Link Image
Target 3 PDB ID 1Z8O Link Image
Target 3 PDB File Show
Target 3 3D Structure
Target 3 Cellular Location Not Available
Target 3 Gene Sequence >1221 bp 
ATGACGACCGTTCCCGATCTCGAAAGCGACTCCTTCCACGTCGACTGGTACCGCACCTAC
GCCGAGCTGCGCGAGACCGCGCCGGTGACGCCGGTGCGCTTCCTCGGCCAGGACGCGTGG
CTGGTCACCGGCTACGACGAGGCGAAGGCCGCGCTGAGCGACCTGCGCCTGAGCAGCGAC
CCGAAGAAGAAGTACCCGGGCGTGGAGGTCGAGTTCCCGGCATACCTCGGTTTCCCCGAG
GACGTGCGGAACTACTTCGCCACCAACATGGGCACCAGCGACCCGCCGACCCACACCCGG
CTGCGCAAGCTGGTGTCGCAGGAGTTCACCGTCCGCCGCGTGGAGGCGATGCGGCCCCGC
GTCGAGCAGATCACCGCGGAGCTGCTCGACGAGGTGGGCGACTCCGGCGTGGTCGACATC
GTCGACCGCTTCGCCCACCCGCTGCCCATCAAGGTCATCTGCGAGCTGCTCGGCGTCGAC
GAGAAGTACCGCGGGGAGTTCGGGCGGTGGAGCTCGGAGATCCTGGTCATGGACCCGGAG
CGGGCCGAACAGCGCGGGCAGGCGGCCAGGGAGGTCGTCAACTTCATCCTCGACCTGGTC
GAGCGCCGCCGCACCGAGCCCGGCGACGACCTGCTGTCCGCGCTGATCAGGGTCCAGGAC
GACGATGACGGTCGGCTCAGCGCCGACGAGCTGACCTCCATCGCGCTGGTGCTGCTGCTG
GCCGGTTTCGAGGCGTCGGTGAGCCTCATCGGGATCGGCACCTACCTGCTGCTCACCCAC
CCGGACCAGGACCAGCTCGCGCTGGTGCGGCGGGACCCGTCGGCGCTGCCCAACGCCGTC
GAGGAGATCCTGCGCTACATCGCTCCGCCGGAGACCACCACGCGCTTCGCCGCGGAGGAG
GTGGAGATCCGGGGTGTCGCGATCCCCCAGTACAGCACGGTGCTGGTCGCGAACGGCGCG
GCCAACCGCGACCCGAAGCAGTTCCCGGACCCCCACCGCTTCGACGTCACCCGCGACACC
CGCGGCCACCTGTCGTTCGGGCAGGGCATCCACTTCTGCATGGGCCGGCCGCTGGCCAAG
CTGGAGGGCGAGGTGGCGCTGCGGGCGCTGTTCGGCCGCTTCCCCGCTCTGTCGCTGGGA
ATCGACGCCGACGACGTGGTGTGGCGGCGTTCGCTGCTGCTGCGGGGCATCGACCACCTA
CCGGTGCGGCTCGACGGATGA
Target 3 GenBank Gene ID
Target 3 GeneCard ID Not Available
Target 3 GenAtlas ID Not Available
Target 3 HGNC ID Not Available
Target 3 Chromosome Location Not Available
Target 3 Locus Not Available
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Cupp-Vickery J, Anderson R, Hatziris Z: Crystal structures of ligand complexes of P450eryF exhibiting homotropic cooperativity. Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3050-5. [PubMed Link Image]
  2. Cupp-Vickery JR, Garcia C, Hofacre A, McGee-Estrada K: Ketoconazole-induced conformational changes in the active site of cytochrome P450eryF. J Mol Biol. 2001 Aug 3;311(1):101-10. [PubMed Link Image]
  3. Haydock SF, Dowson JA, Dhillon N, Roberts GA, Cortes J, Leadlay PF: Cloning and sequence analysis of genes involved in erythromycin biosynthesis in Saccharopolyspora erythraea: sequence similarities between EryG and a family of S-adenosylmethionine-dependent methyltransferases. Mol Gen Genet. 1991 Nov;230(1-2):120-8. [PubMed Link Image]
  4. Weber JM, Leung JO, Swanson SJ, Idler KB, McAlpine JB: An erythromycin derivative produced by targeted gene disruption in Saccharopolyspora erythraea. Science. 1991 Apr 5;252(5002):114-7. [PubMed Link Image]
  5. Cupp-Vickery JR, Poulos TL: Structure of cytochrome P450eryF involved in erythromycin biosynthesis. Nat Struct Biol. 1995 Feb;2(2):144-53. [PubMed Link Image]
Target 3 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.