Structure of PDB 3cv9 Chain A Binding Site BS01

Receptor Information
>3cv9 Chain A (length=401) Species: 1909 (Streptomyces griseolus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PQTTDAPAFPSNRSCPYQLPDGYAQLRDTPGPLHRVTLYDGRQAWVVTKH
EAARKLLGDPRLSSNATDDNFPATSPAFEAVRESPQAFIGLDPPEHGTRR
RMTISEFTVKRIKGMRPEVEEVVHGFLDEMLAAGPTADLVSQFALPVPSM
VICRLLGVPYADHEFFQDASKRLVQSTDAQSALTARNDLAGYLDGLITQF
QTEPGAGLVGALVADQLANGEIDREELISTAMLLLIAGHETTASMTSLSV
ITLLDHPEQYAALRADRSLVPGAVEELLRYLAIADIAGGRVATADIEVEG
QLIRAGEGVIVVNSIANRDGTVYEDPDALDIHRSARHHLAFGFGVHQCLG
QNLARLELEVILNALMDRVPTLRLAVPVEQLVLRPGTTIQGVNELPVTWH
H
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 chain3cv9 Chain A Residue 413 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3cv9 Structure-based design of a highly active vitamin D hydroxylase from Streptomyces griseolus CYP105A1
Resolution1.7 Å
Binding residue
(original residue number in PDB)		F95 I96 H103 R107 L241 A244 G245 T248 T249 A294 R297 A347 F348 H353 C355 G357
Binding residue
(residue number reindexed from 1)		F88 I89 H96 R100 L234 A237 G238 T241 T242 A287 R290 A340 F341 H346 C348 G350
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Q182 A244 E247 T248 T249 A291 C355 L356 G357 E364 I396
Catalytic site (residue number reindexed from 1) Q175 A237 E240 T241 T242 A284 C348 L349 G350 E357 I389
Enzyme Commision number 1.14.15.22: vitamin D 1,25-hydroxylase.
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0016709 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0070640 vitamin D3 metabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3cv9, PDBe:3cv9, PDBj:3cv9
PDBsum3cv9
PubMed18937506
UniProtP18326|CPXE_STRGO Vitamin D3 dihydroxylase (Gene Name=cyp105A1)

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