Structure of PDB 5gnm Chain A

Receptor sequence

>5gnmA (length=399) Species: 2074 (Pseudonocardia autotrophica)

LTTTGTEQHDLFSGTFWQNPHPAYAALRAEDPVRKLALPDGPVWLLTRYA
DVREAFVDPRLSKDWRHTLPEDQRADMPATPTPMMILMDPPDHTRLRKLV
GRSFTVRRMNELEPRITEIADGLLAGLPTDGPVDLMREYAFQIPVQVICE
LLGVPAEDRDDFSAWSSVLVDDSPADDKNAAMGKLHGYLSDLLERKRTEP
DDALLSSLLAVSDEDGDRLSQEELVAMAMLLLIAGHETTVNLIGNGVLAL
LTHPDQRKLLAEDPSLISSAVEEFLRFDSPVSQAPIRFTAEDVTYSGVTI
PAGEMVMLGLAAANRDADWMPEPDRLDITRDASGGVFFGHGIHFCMGAQL
ARLEGRVAIGRLFADRPELALAVGLDELVYRESTLVRGLSRMPVTMGPR

3D structure

• PDB: 5gnm Structural insights into the mechanism of the drastic changes in enzymatic activity of the cytochrome P450 vitamin D3 hydroxylase (CYP107BR1) caused by a mutation distant from the active site
• Chain: A
• Resolution: 2.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D173 A236 E239 T240 T241 V283 C347 M348 G349 E356 V388
• Catalytic site (residue number reindexed from 1): D171 A234 E237 T238 T239 V281 C345 M346 G347 E354 V386
• 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 R99 A236 G237 T240 V283 P287 R289 F339 F340 H345 C347 M348 G349 A353	K63 M85 R97 A234 G235 T238 V281 P285 R287 F337 F338 H343 C345 M346 G347 A351

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:5gnm, PDBe:5gnm, PDBj:5gnm
• PDBsum: 5gnm
• PubMed: 28471358
• UniProt: C4B644|CPVDH_PSEAH Vitamin D(3) 25-hydroxylase (Gene Name=vdh)