Structure of PDB 3a4z Chain B

Receptor sequence
>3a4zB (length=402) Species: 2074 (Pseudonocardia autotrophica) [Search protein sequence]
ALTTTGTEQHDLFSGTFWQNPHPAYAALRAEDPVRKLALPDGPVWLLTRY
ADVREAFVDPRLSKDWRHRLPEDQRADMPATPTPMMILMDPPDHTRLRKL
VGRSFTVRRMNELEPRITEIADGLLAGLPTDGPVDLMREYAFQIPVQVIC
ELLGLPAEDRDDFSAWSSVLVDDSPADDKNAAMGKLHGYLSDLLERKRTE
PDDALLSSLLAVSDMDGDRLSQEELVAMAMLLLIAGHETTVNLIGNGVLA
LLTHPDQRKLLAEDPSLISSAVEEFLRFDSPVSQAPIRFTAEDVTYSGVT
IPAGEMVMLGLAAANRDADWMPEPDRLDITRDASGGVFFGHGIHFCLGAQ
LARLEGRVAIGRLFADRPELALAVGLDELVYRRSTLVRGLSRMPVTMGPR
SA
3D structure
PDB3a4z Structural evidence for enhancement of sequential vitamin D3 hydroxylation activities by directed evolution of cytochrome P450 vitamin D3 hydroxylase
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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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) D172 A235 E238 T239 T240 V282 C346 L347 G348 E355 V387
Enzyme Commision number 1.14.15.15: cholestanetriol 26-monooxygenase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 HEM B K65 H95 R99 A236 T240 T241 L244 V283 P287 R289 F339 F340 H345 C347 G349 A353 K64 H94 R98 A235 T239 T240 L243 V282 P286 R288 F338 F339 H344 C346 G348 A352
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:3a4z, PDBe:3a4z, PDBj:3a4z
PDBsum3a4z
PubMed20667833
UniProtC4B644|CPVDH_PSEAH Vitamin D(3) 25-hydroxylase (Gene Name=vdh)

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