Structure of PDB 1lgf Chain A

Receptor sequence
>1lgfA (length=388) Species: 31958 (Amycolatopsis orientalis) [Search protein sequence]
DPRPLHIRRQGLDPADELLAAGALTRVTAETHWMATAHAVVRQVMGDHQQ
FSTRRRWDPRDEIGGKGIFRPRELVGNLMDYDPPEHTRLRRKLTPGFTLR
KMQRMAPYIEQIVNDRLDEMERAGSPADLIAFVADKVPGAVLCELVGVPR
DDRDMFMKLCHGHLDASLSQKRRAALGDKFSRYLLAMIARERKEPGEGMI
GAVVAEYGDDATDEELRGFCVQVMLAGDDNISGMIGLGVLAMLRHPEQID
AFRGDEQSAQRAVDELIRYLTVPYSPTPRIAREDLTLAGQEIKKGDSVIC
SLPAANRDPALAPDVDRLDVTREPIPHVAFGHGVHHCLGAALARLELRTV
FTELWRRFPALRLADPAQDTEFRLTTPAYGLTELMVAW
3D structure
PDB1lgf Crystal Structure of OxyB, a Cytochrome P450 Implicated in an Oxidative Phenol Coupling Reaction during Vancomycin Biosynthesis.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D175 A236 D239 N240 I241 C347 L348 G349 E356 A388
Catalytic site (residue number reindexed from 1) D165 A226 D229 N230 I231 C337 L338 G339 E346 A378
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 L88 M89 H96 R100 A236 G237 N240 P286 T287 R289 A339 F340 G341 H345 C347 L78 M79 H86 R90 A226 G227 N230 P276 T277 R279 A329 F330 G331 H335 C337
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
Biological Process
GO:0033072 vancomycin biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1lgf, PDBe:1lgf, PDBj:1lgf
PDBsum1lgf
PubMed12207020
UniProtQ8RN04|C5B3_AMYOR Cytochrome P450 165B3 (Gene Name=cyp165B3)

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