Structure of PDB 1lg9 Chain A

Receptor sequence
>1lg9A (length=377) Species: 31958 (Amycolatopsis orientalis) [Search protein sequence]
DPRPLHIRRQGLDPADELLAAGALTRVTIGSGADAETHWMATAHAVVRQV
MGDHQQFSTRRELVGNLMDYDPPEHTRLRRKLTPGFTLRKMQRMAPYIEQ
IVNDRLDEMERAGSPADLIAFVADKVPGAVLCELVGVPRDDRDMFMKLCH
GHLDASLSQKRRAALGDKFSRYLLAMIARERKEPGEGMIGAVVAEYGDDA
TDEELRGFCVQVMLAGDDNISGMIGLGVLAMLRHPEQIDAFRGDEQSAQR
AVDELIRYLTVPYSPTPRIAREDLTLAGQEIKKGDSVICSLPAANRDPAL
APDVDRLDVTREPIPHVAFGHGVHHCLGAALARLELRTVFTELWRRFPAL
RLADPAQDTEFRLTTPAYGLTELMVAW
3D structure
PDB1lg9 Crystal Structure of OxyB, a Cytochrome P450 Implicated in an Oxidative Phenol Coupling Reaction during Vancomycin Biosynthesis.
ChainA
Resolution2.0 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) D154 A215 D218 N219 I220 C326 L327 G328 E335 A367
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 P283 P286 T287 R289 A339 F340 G341 H345 C347 G349 L67 M68 H75 R79 A215 G216 N219 P262 P265 T266 R268 A318 F319 G320 H324 C326 G328
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:1lg9, PDBe:1lg9, PDBj:1lg9
PDBsum1lg9
PubMed12207020
UniProtQ8RN04|C5B3_AMYOR Cytochrome P450 165B3 (Gene Name=cyp165B3)

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