Structure of PDB 3mgx Chain B

Receptor sequence
>3mgxB (length=391) Species: 208443 (Amycolatopsis balhimycina) [Search protein sequence]
AVDLGNPDLYTTLERHARWRELAAEDAMVWSDPGSSPSGFWSVFSHRACA
AVLAPSAPLTSEYGMMIGFDRDHPDNSGGRMMVVSEHEQHRKLRKLVGPL
LSRAAARKLAERVRIEVGDVLGRVLDGEVCDAATAIGPRIPAAVVCEILG
VPAEDEDMLIDLTNHAFGGEDELFDGMTPRQAHTEILVYFDELITARRKE
PGDDLVSTLVTDDDLTIDDVLLNCDNVLIGGNETTRHAITGAVHALATVP
GLLTALRDGSADVDTVVEEVLRWTSPAMHVLRVTTADVTINGRDLPSGTP
VVAWLPAANRDPAEFDDPDTFLPGRKPNRHITFGHGMHHCLGSALARIEL
SVVLRVLAERVSRVDLEREPAWLRAIVVQGYRELPVRFTGR
3D structure
PDB3mgx Structural characterization of oxyd, a cytochrome p450 involved in {beta}-hydroxytyrosine formation in vancomycin biosynthesis
ChainB
Resolution2.1 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) G173 G235 E238 T239 T240 C345 L346 G347 E354 V383
Catalytic site (residue number reindexed from 1) G168 G230 E233 T234 T235 C340 L341 G342 E349 V378
Enzyme Commision number 1.14.14.1: unspecific 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 B M70 M87 V88 H95 R99 G235 G236 T239 T240 V285 R287 T337 F338 H343 C345 G347 A351 M65 M82 V83 H90 R94 G230 G231 T234 T235 V280 R282 T332 F333 H338 C340 G342 A346
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:0016787 hydrolase activity
GO:0020037 heme binding
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:3mgx, PDBe:3mgx, PDBj:3mgx
PDBsum3mgx
PubMed20519494
UniProtQ939Y1

[Back to BioLiP]