Structure of PDB 3u9f Chain H

Receptor sequence
>3u9fH (length=213) Species: 562 (Escherichia coli) [Search protein sequence]
ITGYTTVDISQWHRKEHFEAFQSVAQCTYNQTVQLDITAFLKTVKKNKHK
FYPAFIHILARLMNAHPEFRMAMKDGELVIWDSVHPCYTVFHEQTETFSS
LWSEYHDDFRQFLHIYSQDVACYGENLAYFPKGFIENMFFVSANPWVSFT
SFDLNVANMDNFFAPVFTMGKYYTQGDKVLMPLAIQVHHAVCDGFHVGRM
LNELQQYCDEWQG
3D structure
PDB3u9f The structural basis for substrate versatility of chloramphenicol acetyltransferase CAT(I).
ChainH
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) R14 T168 H189 D193
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 H A29 H193 A25 H189
BS02 CLM H S104 Y133 F134 S146 S100 Y129 F130 S142
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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