Structure of PDB 1q23 Chain J

Receptor sequence
>1q23J (length=212) Species: 562 (Escherichia coli) [Search protein sequence]
ITGYTTVDISQWHRKEHFEAFQSVAQCTYNQTVQLDITAFLKTVKKNKHK
FYPAFIHILARLMNAHPEFRMAMKDGELVIWDSVHPCYTVFHEQTETFSS
LWSEYHDDFRQFLHIYSQDVACYGENLAYFPKGFIENMFFVSANPWVSFT
SFDLNVANMDNFFAPVFTMGKYYTQGDKVLMPLAIQVHHAVCDGFHVGRM
LNELQQYCDEWQ
3D structure
PDB1q23 Crystal structure of Chloramphenicol acetyltransferase I in the apoenzyme form and complexed with fusidic acid at 2.18 A resolution
ChainJ
Resolution2.18 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 FUA J T93 F102 Y133 F134 F138 S146 L158 V160 F166 T89 F98 Y129 F130 F134 S142 L154 V156 F162
BS02 FUA J V28 A29 H193 V24 A25 H189
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:1q23, PDBe:1q23, PDBj:1q23
PDBsum1q23
PubMed
UniProtP62577|CAT_ECOLX Chloramphenicol acetyltransferase (Gene Name=cat)

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