Structure of PDB 3a4h Chain A

Receptor sequence
>3a4hA (length=400) Species: 2074 (Pseudonocardia autotrophica) [Search protein sequence]
TTTGTEQHDLFSGTFWQNPHPAYAALRAEDPVRKLALPDGPVWLLTRYAD
VREAFVDPRLSKDWRHTLPEDQRADMPATPTPMMILMDPPDHTRLRKLVG
RSFTVRRMNELEPRITEIADGLLAGLPTDGPVDLMREYAFQIPVQVICEL
LGVPAEDRDDFSAWSSVLVDDSPADDKNAAMGKLHGYLSDLLERKRTEPD
DALLSSLLAVSDEDGDRLSQEELVAMAMLLLIAGHETTVNLIGNGVLALL
THPDQRKLLAEDPSLISSAVEEFLRFDSPVSQAPIRFTAEDVTYSGVTIP
AGEMVMLGLAAANRDADWMPEPDRLDITRDASGGVFFGHGIHFCLGAQLA
RLEGRVAIGRLFADRPELALAVGLDELVYRESTLVRGLSRMPVTMGPRSA
3D structure
PDB3a4h Structural evidence for enhancement of sequential vitamin D3 hydroxylation activities by directed evolution of cytochrome P450 vitamin D3 hydroxylase
ChainA
Resolution3.06 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) D170 A233 E236 T237 T238 V280 C344 L345 G346 E353 V385
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 F106 A236 G237 T240 T241 V283 P287 R289 F339 F340 G341 H345 C347 L348 G349 A353 K62 M84 I85 H92 R96 F103 A233 G234 T237 T238 V280 P284 R286 F336 F337 G338 H342 C344 L345 G346 A350
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:3a4h, PDBe:3a4h, PDBj:3a4h
PDBsum3a4h
PubMed20667833
UniProtC4B644|CPVDH_PSEAH Vitamin D(3) 25-hydroxylase (Gene Name=vdh)

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