Structure of PDB 3u9f Chain F

Receptor sequence
>3u9fF (length=211) Species: 562 (Escherichia coli) [Search protein sequence]
GYTTVDISQWHRKEHFEAFQSVAQCTYNQTVQLDITAFLKTVKKNKHKFY
PAFIHILARLMNAHPEFRMAMKDGELVIWDSVHPCYTVFHEQTETFSSLW
SEYHDDFRQFLHIYSQDVACYGENLAYFPKGFIENMFFVSANPWVSFTSF
DLNVANMDNFFAPVFTMGKYYTQGDKVLMPLAIQVHHAVCDGFHVGRMLN
ELQQYCDEWQG
3D structure
PDB3u9f The structural basis for substrate versatility of chloramphenicol acetyltransferase CAT(I).
ChainF
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) R18 T172 H193 D197
Catalytic site (residue number reindexed from 1) R12 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 CLM F F25 H193 F19 H187
BS02 CLM F S104 Y133 S146 F166 V170 S98 Y127 S140 F160 V164
Gene Ontology
Molecular Function
GO:0008811 chloramphenicol O-acetyltransferase activity
GO:0016746 acyltransferase activity
Biological Process
GO:0046677 response to antibiotic

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3u9f, PDBe:3u9f, PDBj:3u9f
PDBsum3u9f
PubMed22294317
UniProtP62577|CAT_ECOLX Chloramphenicol acetyltransferase (Gene Name=cat)

[Back to BioLiP]