Structure of PDB 3g1r Chain B Binding Site BS02

Receptor Information
>3g1r Chain B (length=325) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DLSAASHRIPLSDGNSIPIIGLGTYSEPKSTPKGACATSVKVAIDTGYRH
IDGAYIYQNEHEVGEAIREKIAEGKVRREDIFYCGKLWATNHVPEMVRPT
LERTLRVLQLDYVDLYIIEVPMAFKPGDEIYPRDENGKWLYHKSNLCATW
EAMEACKDAGLVKSLGVSNFNRRQLELILNKPGLKHKPVSNQVECHPYFT
QPKLLKFCQQHDIVITAYSPLGTSRNPIWVNVSSPPLLKDALLNSLGKRY
NKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEA
LNKNVRFVELLMWRDHPEYPFHDEY
Ligand information
Ligand IDFIT
InChIInChI=1S/C23H36N2O2/c1-21(2,3)25-20(27)17-8-7-15-14-6-9-18-23(5,13-11-19(26)24-18)16(14)10-12-22(15,17)4/h11,13-18H,6-10,12H2,1-5H3,(H,24,26)(H,25,27)/t14-,15-,16-,17+,18+,22-,23+/m0/s1
InChIKeyDBEPLOCGEIEOCV-WSBQPABSSA-N
SMILES
SoftwareSMILES
CACTVS 3.341CC(C)(C)NC(=O)[CH]1CC[CH]2[CH]3CC[CH]4NC(=O)C=C[C]4(C)[CH]3CC[C]12C
ACDLabs 10.04O=C(NC(C)(C)C)C2C1(CCC3C(C1CC2)CCC4NC(=O)C=CC34C)C
OpenEye OEToolkits 1.5.0CC12CCC3C(C1CCC2C(=O)NC(C)(C)C)CCC4C3(C=CC(=O)N4)C
OpenEye OEToolkits 1.5.0C[C@]12CC[C@H]3[C@H]([C@@H]1CC[C@@H]2C(=O)NC(C)(C)C)CC[C@@H]4[C@@]3(C=CC(=O)N4)C
CACTVS 3.341CC(C)(C)NC(=O)[C@H]1CC[C@H]2[C@@H]3CC[C@H]4NC(=O)C=C[C@]4(C)[C@H]3CC[C@]12C
FormulaC23 H36 N2 O2
Name(4aR,4bS,6aS,7S,9aS,9bS,11aR)-N-tert-butyl-4a,6a-dimethyl-2-oxo-2,4a,4b,5,6,6a,7,8,9,9a,9b,10,11,11a-tetradecahydro-1H-indeno[5,4-f]quinoline-7-carboxamide;
FINASTERIDE
ChEMBLCHEMBL710
DrugBankDB01216
ZINCZINC000003782599
PDB chain3g1r Chain B Residue 327 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3g1r Inhibition of human steroid 5beta-reductase (AKR1D1) by finasteride and structure of the enzyme-inhibitor complex.
Resolution1.701 Å
Binding residue
(original residue number in PDB)		Y26 Y58 W89 E120 Y132 W140 W230 M313
Binding residue
(residue number reindexed from 1)		Y25 Y57 W88 E119 Y131 W139 W229 M312
Annotation score1
Binding affinityMOAD: Ki=2.1uM
Enzymatic activity
Catalytic site (original residue number in PDB) D53 Y58 K87 E120
Catalytic site (residue number reindexed from 1) D52 Y57 K86 E119
Enzyme Commision number 1.3.1.3: Delta(4)-3-oxosteroid 5beta-reductase.
Gene Ontology
Molecular Function
GO:0004032 aldose reductase (NADPH) activity
GO:0004033 aldo-keto reductase (NADPH) activity
GO:0005496 steroid binding
GO:0005515 protein binding
GO:0016229 steroid dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0047086 ketosteroid monooxygenase activity
GO:0047787 Delta4-3-oxosteroid 5beta-reductase activity
Biological Process
GO:0006699 bile acid biosynthetic process
GO:0006707 cholesterol catabolic process
GO:0007586 digestion
GO:0008202 steroid metabolic process
GO:0008207 C21-steroid hormone metabolic process
GO:0008209 androgen metabolic process
GO:0016042 lipid catabolic process
GO:0030573 bile acid catabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3g1r, PDBe:3g1r, PDBj:3g1r
PDBsum3g1r
PubMed19515843
UniProtP51857|AK1D1_HUMAN Aldo-keto reductase family 1 member D1 (Gene Name=AKR1D1)

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