Structure of PDB 1qca Chain A

Receptor sequence
>1qcaA (length=211) Species: 623 (Shigella flexneri) [Search protein sequence]
MNYTKFDVKNWVRREHFEFYRHRLPCGFSLTSKIDITTLKKSLDDSAYKF
YPVMIYLIAQAVNQFDELRMAIKDDELIVWDSVDPCFTVFHQETETFSAL
SCPYSSDIDQFMVNYLSVMERYKSDTKLFPQGPENHLFISALPWVNFDSF
NLNVANFTDFFAPVITMAKYQQEGDRLLLPLSVQVHHAVCDGFHVARFIN
RLQELCNSKLK
3D structure
PDB1qca Steroid recognition by chloramphenicol acetyltransferase: engineering and structural analysis of a high affinity fusidic acid binding site.
ChainA
Resolution2.2 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 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 CO A E23 H27 E18 H22
BS02 FUA A C92 F103 F135 F146 F168 C86 F97 F129 F138 F160 MOAD: Ki=5.4uM
PDBbind-CN: -logKd/Ki=5.27,Ki=5.4uM
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:1qca, PDBe:1qca, PDBj:1qca
PDBsum1qca
PubMed7500366
UniProtP00484|CAT3_ECOLX Chloramphenicol acetyltransferase 3 (Gene Name=cat3)

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