Structure of PDB 3a4g Chain A Binding Site BS01

Receptor Information
>3a4g Chain A (length=395) Species: 2074 (Pseudonocardia autotrophica) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EQHDLFSGTFWQNPHPAYAALRAEDPVRKLALPDGPVWLLTRYADVREAF
VDPRLSKDWRHTLPEDQRADMPATPTPMMILMDPPDHTRLRKLVGRSFTV
RRMNELEPRITEIADGLLAGLPTDGPVDLMREYAFQIPVQVICELLGVPA
EDRDDFSAWSSVLVDDSPADDKNAAMGKLHGYLSDLLERKRTEPDDALLS
SLLAVSDEDGDRLSQEELVAMAMLLLIAGHETTVNLIGNGVLALLTHPDQ
RKLLAEDPSLISSAVEEFLRFDSPVSQAPIRFTAEDVTYSGVTIPAGEMV
MLGLAAANRDADWMPEPDRLDITRDASGGVFFGHGIHFCLGAQLARLEGR
VAIGRLFADRPELALAVGLDELVYRESTLVRGLSRMPVTMGPRSA
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 chain3a4g 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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PDB3a4g Structural evidence for enhancement of sequential vitamin D3 hydroxylation activities by directed evolution of cytochrome P450 vitamin D3 hydroxylase
Resolution1.75 Å
Binding residue
(original residue number in PDB)		K65 M87 I88 H95 R99 A236 G237 T240 T241 V283 P287 R289 F339 F340 H345 C347 L348 G349 A353
Binding residue
(residue number reindexed from 1)		K57 M79 I80 H87 R91 A228 G229 T232 T233 V275 P279 R281 F331 F332 H337 C339 L340 G341 A345
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) D165 A228 E231 T232 T233 V275 C339 L340 G341 E348 V380
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

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Molecular Function
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Cellular Component
External links
PDB RCSB:3a4g, PDBe:3a4g, PDBj:3a4g
PDBsum3a4g
PubMed20667833
UniProtC4B644|CPVDH_PSEAH Vitamin D(3) 25-hydroxylase (Gene Name=vdh)

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