Structure of PDB 3n9y Chain B Binding Site BS01

Receptor Information
>3n9y Chain B (length=470) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PRPFNEIPSPGDNGWLNLYHFWRETGTHKVHLHHVQNFQKYGPIYREKLG
NVESVYVIDPEDVALLFKSEGPNPERFLIPPWVAYHQYYQRPIGVLLKKS
AAWKKDRVALNQEVMAPEATKNFLPLLDAVSRDFVSVLHRRIKKAGSGNY
SGDISDDLFRFAFESITNVIFGERQGMLEEVVNPEAQRFIDAIYQMFHTS
VPMLNLPPDLFRLFRTKTWKDHVAAWDVIFSKADIYTQNFYWELRQKGSV
HHDYRGILYRLLGDSKMSFEDIKANVTEMLAGGVDTTSMTLQWHLYEMAR
NLKVQDMLRAEVLAARHQAQGDMATMLQLVPLLKASIKETLRLHPISVTL
QRYLVNDLVLRDYMIPAKTLVQVAIYALGREPTFFFDPENFDPTRWLSKD
KNITYFRNLGFGWGVRQCLGRRIAELEMTIFLINMLENFRVEIQHLSDVG
TTFNLILMPEKPISFTFWPF
Ligand information
Ligand IDHEM
InChIInChI=1S/C34H34N4O4.Fe/c1-7-21-17(3)25-13-26-19(5)23(9-11-33(39)40)31(37-26)16-32-24(10-12-34(41)42)20(6)28(38-32)15-30-22(8-2)18(4)27(36-30)14-29(21)35-25;/h7-8,13-16H,1-2,9-12H2,3-6H3,(H4,35,36,37,38,39,40,41,42);/q;+2/p-2/b25-13-,26-13-,27-14-,28-15-,29-14-,30-15-,31-16-,32-16-;
InChIKeyKABFMIBPWCXCRK-RGGAHWMASA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6Cc1c2n3c(c1CCC(=O)O)C=C4C(=C(C5=[N]4[Fe]36[N]7=C(C=C8N6C(=C5)C(=C8C)C=C)C(=C(C7=C2)C)C=C)C)CCC(=O)O
CACTVS 3.385CC1=C(CCC(O)=O)C2=Cc3n4[Fe]5|6|N2=C1C=c7n5c(=CC8=N|6C(=Cc4c(C)c3CCC(O)=O)C(=C8C=C)C)c(C)c7C=C
ACDLabs 12.01C=1c3c(c(c4C=C5C(=C(C=6C=C7C(=C(C8=CC=2C(=C(C=1N=2[Fe](n34)(N5=6)N78)CCC(=O)O)C)\C=C)C)\C=C)C)C)CCC(=O)O
FormulaC34 H32 Fe N4 O4
NamePROTOPORPHYRIN IX CONTAINING FE;
HEME
ChEMBL
DrugBankDB18267
ZINC
PDB chain3n9y Chain B Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3n9y Structural basis for pregnenolone biosynthesis by the mitochondrial monooxygenase system.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		R81 R112 M284 G287 T291 I351 R357 G415 F416 R421 Q422 C423 G425
Binding residue
(residue number reindexed from 1)		R76 R107 M279 G282 T286 I346 R352 G410 F411 R416 Q417 C418 G420
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) T291 F416 C423
Catalytic site (residue number reindexed from 1) T286 F411 C418
Enzyme Commision number 1.14.15.6: cholesterol monooxygenase (side-chain-cleaving).
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0005515 protein binding
GO:0008386 cholesterol monooxygenase (side-chain-cleaving) activity
GO:0008395 steroid hydroxylase activity
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0006694 steroid biosynthetic process
GO:0006700 C21-steroid hormone biosynthetic process
GO:0006704 glucocorticoid biosynthetic process
GO:0008203 cholesterol metabolic process
GO:0008207 C21-steroid hormone metabolic process
GO:0016125 sterol metabolic process
GO:0034650 cortisol metabolic process
GO:0042359 vitamin D metabolic process
GO:0042446 hormone biosynthetic process
GO:0071375 cellular response to peptide hormone stimulus
GO:1901615 organic hydroxy compound metabolic process
Cellular Component
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane
GO:0005759 mitochondrial matrix

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3n9y, PDBe:3n9y, PDBj:3n9y
PDBsum3n9y
PubMed21636783
UniProtP05108|CP11A_HUMAN Cholesterol side-chain cleavage enzyme, mitochondrial (Gene Name=CYP11A1)

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