Structure of PDB 5ofq Chain D

Receptor sequence
>5ofqD (length=387) Species: 592022 (Priestia megaterium DSM 319) [Search protein sequence]
LIPMQEIKSVEQQLYPFDIYNSLRQEAPIRYDESRNCWDVFDYETVKYIL
KNPSLFSSKRAMEERQESILMMDPPKHTKLRNLVNKAFTPRAIQHLEGHI
EEIADYLLDEVSSKEKFDIVEDFAGPLPIIVIAELLGVPIQDRALFKKYS
DDLVSGAENNSDEAFAKMMQKRNEGVIFLQGYFKEIIAERQQNKQEDLIS
LLLEAEIDGEHLTEEEVLGFCILLLVAGNETTTNLITNGVRYMTEDVDVQ
NEVRRDISLVPNLVEETLRYYPPIQAIGRIAAEDVELGECKIKRGQQVIS
WAASANRDSAKFEWPDTFVVHRKTNPHVSFGFGIHFCLGAPLARMEGKIA
FTKLLEKGGFSKVQNQSLKPIDSPFVFGVKKYEIAFN
3D structure
PDB5ofq Biochemical and structural characterization of CYP109A2, a vitamin D3 25-hydroxylase from Bacillus megaterium.
ChainD
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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) S155 A227 E230 T231 T232 C337 L338 G339 E346 V376
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 D I83 H91 R95 L238 A241 G242 T245 T246 P287 I291 R293 S343 F344 H349 C351 G353 A357 I69 H77 R81 L224 A227 G228 T231 T232 P273 I277 R279 S329 F330 H335 C337 G339 A343
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

[Back to BioLiP]