Structure of PDB 3a4h Chain A Binding Site BS01

Receptor Information
>3a4h Chain A (length=400) Species: 2074 (Pseudonocardia autotrophica) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TTTGTEQHDLFSGTFWQNPHPAYAALRAEDPVRKLALPDGPVWLLTRYAD
VREAFVDPRLSKDWRHTLPEDQRADMPATPTPMMILMDPPDHTRLRKLVG
RSFTVRRMNELEPRITEIADGLLAGLPTDGPVDLMREYAFQIPVQVICEL
LGVPAEDRDDFSAWSSVLVDDSPADDKNAAMGKLHGYLSDLLERKRTEPD
DALLSSLLAVSDEDGDRLSQEELVAMAMLLLIAGHETTVNLIGNGVLALL
THPDQRKLLAEDPSLISSAVEEFLRFDSPVSQAPIRFTAEDVTYSGVTIP
AGEMVMLGLAAANRDADWMPEPDRLDITRDASGGVFFGHGIHFCLGAQLA
RLEGRVAIGRLFADRPELALAVGLDELVYRESTLVRGLSRMPVTMGPRSA
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 chain3a4h Chain A Residue 412 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3a4h Structural evidence for enhancement of sequential vitamin D3 hydroxylation activities by directed evolution of cytochrome P450 vitamin D3 hydroxylase
Resolution3.06 Å
Binding residue
(original residue number in PDB)		K65 M87 I88 H95 R99 F106 A236 G237 T240 T241 V283 P287 R289 F339 F340 G341 H345 C347 L348 G349 A353
Binding residue
(residue number reindexed from 1)		K62 M84 I85 H92 R96 F103 A233 G234 T237 T238 V280 P284 R286 F336 F337 G338 H342 C344 L345 G346 A350
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D173 A236 E239 T240 T241 V283 C347 L348 G349 E356 V388
Catalytic site (residue number reindexed from 1) D170 A233 E236 T237 T238 V280 C344 L345 G346 E353 V385
Enzyme Commision number 1.14.15.15: cholestanetriol 26-monooxygenase.
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:0020037 heme binding
GO:0046872 metal ion binding
GO:0047748 cholestanetetraol 26-dehydrogenase activity
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
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Cellular Component
External links
PDB RCSB:3a4h, PDBe:3a4h, PDBj:3a4h
PDBsum3a4h
PubMed20667833
UniProtC4B644|CPVDH_PSEAH Vitamin D(3) 25-hydroxylase (Gene Name=vdh)

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