Structure of PDB 3a4g Chain A

Receptor sequence
>3a4gA (length=395) Species: 2074 (Pseudonocardia autotrophica) [Search protein sequence]
EQHDLFSGTFWQNPHPAYAALRAEDPVRKLALPDGPVWLLTRYADVREAF
VDPRLSKDWRHTLPEDQRADMPATPTPMMILMDPPDHTRLRKLVGRSFTV
RRMNELEPRITEIADGLLAGLPTDGPVDLMREYAFQIPVQVICELLGVPA
EDRDDFSAWSSVLVDDSPADDKNAAMGKLHGYLSDLLERKRTEPDDALLS
SLLAVSDEDGDRLSQEELVAMAMLLLIAGHETTVNLIGNGVLALLTHPDQ
RKLLAEDPSLISSAVEEFLRFDSPVSQAPIRFTAEDVTYSGVTIPAGEMV
MLGLAAANRDADWMPEPDRLDITRDASGGVFFGHGIHFCLGAQLARLEGR
VAIGRLFADRPELALAVGLDELVYRESTLVRGLSRMPVTMGPRSA
3D structure
PDB3a4g Structural evidence for enhancement of sequential vitamin D3 hydroxylation activities by directed evolution of cytochrome P450 vitamin D3 hydroxylase
ChainA
Resolution1.75 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) D165 A228 E231 T232 T233 V275 C339 L340 G341 E348 V380
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 A K65 M87 I88 H95 R99 A236 G237 T240 T241 V283 P287 R289 F339 F340 H345 C347 L348 G349 A353 K57 M79 I80 H87 R91 A228 G229 T232 T233 V275 P279 R281 F331 F332 H337 C339 L340 G341 A345
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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