Structure of PDB 3vrm Chain A

Receptor sequence

>3vrmA (length=402) Species: 2074 (Pseudonocardia autotrophica)

ALTTTGTEQHDLFSGTFWQNPHPAYAALRAEDPVRKLALPDGPVWLLTRY
ADVREAFVDPRLSKDWRHTLPEDQRADMPATPTPMMILMDPPDHTRLRKL
VGRSFAVRRMNELEPRITEIADGLLAGLPTDGPVDLMREYAFQIPVQVIC
ELLGVPAEDRDDFSAWSSVLVDDSPADDKNAAMGKLHGYLSDLLERKRTE
PDDALLSSLLAVSDEDGDRLSQEELVAMAMLLLIAGHETTVNLIGNGVLA
LLTHPDQRKLLAEDPSLISSAVEEFLRFDSPVSQAPIRFTAEDVTYSGVT
IPAGEMVMLGLAAANRDADWMPEPDRLDITRDASGGVFFGHGIHFCLGAQ
LARLEGRVAIGRLFADRPELALAVGLDELVYRESTLVRGLSRMPVTMGPR
SA

3D structure

• PDB: 3vrm A single mutation at the ferredoxin binding site of p450 vdh enables efficient biocatalytic production of 25-hydroxyvitamin d3.
• Chain: A
• Resolution: 2.57 Å

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	A	I88 H95 R99 L232 L233 A236 T240 T241 V283 R289 F339 F340 G341 H345 C347 G349 A353	I87 H94 R98 L231 L232 A235 T239 T240 V282 R288 F338 F339 G340 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

External links

• PDB: RCSB:3vrm, PDBe:3vrm, PDBj:3vrm
• PDBsum: 3vrm
• PubMed: 24115473
• UniProt: C4B644|CPVDH_PSEAH Vitamin D(3) 25-hydroxylase (Gene Name=vdh)