Structure of PDB 3u9f Chain L

Receptor sequence
>3u9fL (length=216) Species: 562 (Escherichia coli) [Search protein sequence]
EKKITGYTTVDISQWHRKEHFEAFQSVAQCTYNQTVQLDITAFLKTVKKN
KHKFYPAFIHILARLMNAHPEFRMAMKDGELVIWDSVHPCYTVFHEQTET
FSSLWSEYHDDFRQFLHIYSQDVACYGENLAYFPKGFIENMFFVSANPWV
SFTSFDLNVANMDNFFAPVFTMGKYYTQGDKVLMPLAIQVHHAVCDGFHV
GRMLNELQQYCDEWQG
3D structure
PDB3u9f The structural basis for substrate versatility of chloramphenicol acetyltransferase CAT(I).
ChainL
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) R17 T171 H192 D196
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 L C31 H193 C30 H192
BS02 CLM L F102 S104 Y133 F134 S146 L158 F166 F101 S103 Y132 F133 S145 L157 F165
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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