Structure of PDB 1cla Chain A

Receptor sequence
>1claA (length=213) Species: 562 (Escherichia coli) [Search protein sequence]
MNYTKFDVKNWVRREHFEFYRHRLPCGFSLTSKIDITTLKKSLDDSAYKF
YPVMIYLIAQAVNQFDELRMAIKDDELIVWDSVDPQFTVFHQETETFSAL
SCPYSSDIDQFMVNYLSVMERYKSDTKLFPQGVTPENHLNIAALPWVNFD
SFNLNVANFTDYFAPIITMAKYQQEGDRLLLPLSVQVHHAVCDGFHVARF
INRLQELCNSKLK
3D structure
PDB1cla Evidence for transition-state stabilization by serine-148 in the catalytic mechanism of chloramphenicol acetyltransferase.
ChainA
Resolution2.34 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 T174 H195 D199
Catalytic site (residue number reindexed from 1) R13 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 CO A E23 H27 E18 H22
BS02 CLM A F135 L160 F129 L154
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:1cla, PDBe:1cla, PDBj:1cla
PDBsum1cla
PubMed2109633
UniProtP00484|CAT3_ECOLX Chloramphenicol acetyltransferase 3 (Gene Name=cat3)

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