Structure of PDB 3o1a Chain A

Receptor sequence
>3o1aA (length=383) Species: 1867 (Actinoplanes teichomyceticus) [Search protein sequence]
ALPLPHQRLRLDPVPEFEELQKAGPLHEYDTEPGMDGRKQWLVTGHDEVR
AILADHERFSSMRPVDDEADRALLPGILQAYDPPDHTRLRRTVAPAYSAR
RMERLRPRIEEIVEECLDDFESVGAPVDFVRHAAWPIPAYIACEFLGVPR
DDQAELSRMIRESRESRLPRQRTLSGLGIVNYTKRLTSGKRRDPGDGMIG
VIVREHGAEISDEELAGLAEGNLIMAAEQMAAQLAVAVLLLVTHPDQMAL
LREKPELIDSATEEVLRHASIVEAPAPRVALADVRMAGRDIHAGDVLTCS
MLATNRAPGDRFDITREKATHMAFGHGIHHCIGAPLARLQLRVALPAVVG
RFPSLRLAVPEEDLRFKPGRPAPFAVEELPLEW
3D structure
PDB3o1a Structural characterization of CYP165D3, a cytochrome P450 involved in phenolic coupling in teicoplanin biosynthesis.
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E166 M226 E229 Q230 M231 V273 C332 I333 G334 Q341 P374
Catalytic site (residue number reindexed from 1) E165 M225 E228 Q229 M230 V272 C331 I332 G333 Q340 P373
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 A L79 Q80 H87 R91 Y98 M226 A227 M231 V273 P276 A277 R279 A324 F325 H330 C332 I333 G334 L78 Q79 H86 R90 Y97 M225 A226 M230 V272 P275 A276 R278 A323 F324 H329 C331 I332 G333
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:0016746 acyltransferase activity
GO:0016757 glycosyltransferase activity
GO:0016874 ligase activity
GO:0020037 heme binding
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:3o1a, PDBe:3o1a, PDBj:3o1a
PDBsum3o1a
PubMed20974107
UniProtQ6ZZI7

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