Structure of PDB 3u9f Chain M

Receptor sequence
>3u9fM (length=211) Species: 562 (Escherichia coli) [Search protein sequence]
GYTTVDISQWHRKEHFEAFQSVAQCTYNQTVQLDITAFLKTVKKNKHKFY
PAFIHILARLMNAHPEFRMAMKDGELVIWDSVHPCYTVFHEQTETFSSLW
SEYHDDFRQFLHIYSQDVACYGENLAYFPKGFIENMFFVSANPWVSFTSF
DLNVANMDNFFAPVFTMGKYYTQGDKVLMPLAIQVHHAVCDGFHVGRMLN
ELQQYCDEWQG
3D structure
PDB3u9f The structural basis for substrate versatility of chloramphenicol acetyltransferase CAT(I).
ChainM
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R18 T172 H193 D197
Catalytic site (residue number reindexed from 1) R12 T166 H187 D191
Enzyme Commision number 2.3.1.28: chloramphenicol O-acetyltransferase.
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 CLM M F102 S104 Y133 S146 F166 F96 S98 Y127 S140 F160
BS02 CLM M F25 H193 F19 H187
Gene Ontology
Molecular Function
GO:0008811 chloramphenicol O-acetyltransferase activity
GO:0016746 acyltransferase activity
Biological Process
GO:0046677 response to antibiotic

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Molecular Function
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Biological Process
External links
PDB RCSB:3u9f, PDBe:3u9f, PDBj:3u9f
PDBsum3u9f
PubMed22294317
UniProtP62577|CAT_ECOLX Chloramphenicol acetyltransferase (Gene Name=cat)

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