Structure of PDB 5ofq Chain A

Receptor sequence
>5ofqA (length=386) Species: 592022 (Priestia megaterium DSM 319) [Search protein sequence]
IPMQEIKSVEQQLYPFDIYNSLRQEAPIRYDESRNCWDVFDYETVKYILK
NPSLFSSKRAMEERQESILMMDPPKHTKLRNLVNKAFTPRAIQHLEGHIE
EIADYLLDEVSSKEKFDIVEDFAGPLPIIVIAELLGVPIQDRALFKKYSD
DLVSGAENNSDEAFAKMMQKRNEGVIFLQGYFKEIIAERQQNKQEDLISL
LLEAEIDGEHLTEEEVLGFCILLLVAGNETTTNLITNGVRYMTEDVDVQN
EVRRDISLVPNLVEETLRYYPPIQAIGRIAAEDVELGECKIKRGQQVISW
AASANRDSAKFEWPDTFVVHRKTNPHVSFGFGIHFCLGAPLARMEGKIAF
TKLLEKGGFSKVQNQSLKPIDSPFVFGVKKYEIAFN
3D structure
PDB5ofq Biochemical and structural characterization of CYP109A2, a vitamin D3 25-hydroxylase from Bacillus megaterium.
ChainA
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S169 A241 E244 T245 T246 C351 L352 G353 E360 V390
Catalytic site (residue number reindexed from 1) S154 A226 E229 T230 T231 C336 L337 G338 E345 V375
Enzyme Commision number 1.14.-.-
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 I83 L84 H91 R95 A241 G242 T245 T246 I291 R293 S343 F344 H349 C351 G353 I68 L69 H76 R80 A226 G227 T230 T231 I276 R278 S328 F329 H334 C336 G338
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

View graph for
Molecular Function
External links
PDB RCSB:5ofq, PDBe:5ofq, PDBj:5ofq
PDBsum5ofq
PubMed28940959
UniProtD5DF88

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