3U9F

Structure of CATI in complex with chloramphenicol

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
AMR Gene: CARD Annotation
AMR Gene Family: CARD Annotation
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
I	d3u9fi_	Alpha and beta proteins (a/b)	CoA-dependent acyltransferases	CoA-dependent acyltransferases	CAT-like	Chloramphenicol acetyltransferase, CAT	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
K	d3u9fk_	Alpha and beta proteins (a/b)	CoA-dependent acyltransferases	CoA-dependent acyltransferases	CAT-like	Chloramphenicol acetyltransferase, CAT	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
Q [auth R]	d3u9fr_	Alpha and beta proteins (a/b)	CoA-dependent acyltransferases	CoA-dependent acyltransferases	CAT-like	Chloramphenicol acetyltransferase, CAT	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
R [auth S]	d3u9fs_	Alpha and beta proteins (a/b)	CoA-dependent acyltransferases	CoA-dependent acyltransferases	CAT-like	Chloramphenicol acetyltransferase, CAT	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d3u9fa_	Alpha and beta proteins (a/b)	CoA-dependent acyltransferases	CoA-dependent acyltransferases	CAT-like	Chloramphenicol acetyltransferase, CAT	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d3u9fb_	Alpha and beta proteins (a/b)	CoA-dependent acyltransferases	CoA-dependent acyltransferases	CAT-like	Chloramphenicol acetyltransferase, CAT	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d3u9fc_	Alpha and beta proteins (a/b)	CoA-dependent acyltransferases	CoA-dependent acyltransferases	CAT-like	Chloramphenicol acetyltransferase, CAT	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
D	d3u9fd_	Alpha and beta proteins (a/b)	CoA-dependent acyltransferases	CoA-dependent acyltransferases	CAT-like	Chloramphenicol acetyltransferase, CAT	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
E	d3u9fe_	Alpha and beta proteins (a/b)	CoA-dependent acyltransferases	CoA-dependent acyltransferases	CAT-like	Chloramphenicol acetyltransferase, CAT	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
F	d3u9ff_	Alpha and beta proteins (a/b)	CoA-dependent acyltransferases	CoA-dependent acyltransferases	CAT-like	Chloramphenicol acetyltransferase, CAT	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
G	d3u9fg_	Alpha and beta proteins (a/b)	CoA-dependent acyltransferases	CoA-dependent acyltransferases	CAT-like	Chloramphenicol acetyltransferase, CAT	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
H	d3u9fh_	Alpha and beta proteins (a/b)	CoA-dependent acyltransferases	CoA-dependent acyltransferases	CAT-like	Chloramphenicol acetyltransferase, CAT	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
J	d3u9fj_	Alpha and beta proteins (a/b)	CoA-dependent acyltransferases	CoA-dependent acyltransferases	CAT-like	Chloramphenicol acetyltransferase, CAT	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
L	d3u9fl_	Alpha and beta proteins (a/b)	CoA-dependent acyltransferases	CoA-dependent acyltransferases	CAT-like	Chloramphenicol acetyltransferase, CAT	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
M	d3u9fm_	Alpha and beta proteins (a/b)	CoA-dependent acyltransferases	CoA-dependent acyltransferases	CAT-like	Chloramphenicol acetyltransferase, CAT	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
N	d3u9fn_	Alpha and beta proteins (a/b)	CoA-dependent acyltransferases	CoA-dependent acyltransferases	CAT-like	Chloramphenicol acetyltransferase, CAT	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
O	d3u9fo_	Alpha and beta proteins (a/b)	CoA-dependent acyltransferases	CoA-dependent acyltransferases	CAT-like	Chloramphenicol acetyltransferase, CAT	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
P	d3u9fp_	Alpha and beta proteins (a/b)	CoA-dependent acyltransferases	CoA-dependent acyltransferases	CAT-like	Chloramphenicol acetyltransferase, CAT	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
I	SCOP2B Superfamily	CoA-dependent acyltransferases	8069085	3000272	SCOP2B (2022-06-29)
K	SCOP2B Superfamily	CoA-dependent acyltransferases	8069085	3000272	SCOP2B (2022-06-29)
Q [auth R]	SCOP2B Superfamily	CoA-dependent acyltransferases	8069085	3000272	SCOP2B (2022-06-29)
R [auth S]	SCOP2B Superfamily	CoA-dependent acyltransferases	8069085	3000272	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	CoA-dependent acyltransferases	8069085	3000272	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	CoA-dependent acyltransferases	8069085	3000272	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	CoA-dependent acyltransferases	8069085	3000272	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	CoA-dependent acyltransferases	8069085	3000272	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	CoA-dependent acyltransferases	8069085	3000272	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	CoA-dependent acyltransferases	8069085	3000272	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	CoA-dependent acyltransferases	8069085	3000272	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	CoA-dependent acyltransferases	8069085	3000272	SCOP2B (2022-06-29)
J	SCOP2B Superfamily	CoA-dependent acyltransferases	8069085	3000272	SCOP2B (2022-06-29)
L	SCOP2B Superfamily	CoA-dependent acyltransferases	8069085	3000272	SCOP2B (2022-06-29)
M	SCOP2B Superfamily	CoA-dependent acyltransferases	8069085	3000272	SCOP2B (2022-06-29)
N	SCOP2B Superfamily	CoA-dependent acyltransferases	8069085	3000272	SCOP2B (2022-06-29)
O	SCOP2B Superfamily	CoA-dependent acyltransferases	8069085	3000272	SCOP2B (2022-06-29)
P	SCOP2B Superfamily	CoA-dependent acyltransferases	8069085	3000272	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
I	CAT	e3u9fI1	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: CAT	ECOD (1.6)
K	CAT	e3u9fK1	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: CAT	ECOD (1.6)
Q [auth R]	CAT	e3u9fR1	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: CAT	ECOD (1.6)
R [auth S]	CAT	e3u9fS1	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: CAT	ECOD (1.6)
A	CAT	e3u9fA1	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: CAT	ECOD (1.6)
B	CAT	e3u9fB1	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: CAT	ECOD (1.6)
C	CAT	e3u9fC1	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: CAT	ECOD (1.6)
D	CAT	e3u9fD1	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: CAT	ECOD (1.6)
E	CAT	e3u9fE1	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: CAT	ECOD (1.6)
F	CAT	e3u9fF1	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: CAT	ECOD (1.6)
G	CAT	e3u9fG1	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: CAT	ECOD (1.6)
H	CAT	e3u9fH1	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: CAT	ECOD (1.6)
J	CAT	e3u9fJ1	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: CAT	ECOD (1.6)
L	CAT	e3u9fL1	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: CAT	ECOD (1.6)
M	CAT	e3u9fM1	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: CAT	ECOD (1.6)
N	CAT	e3u9fN1	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: CAT	ECOD (1.6)
O	CAT	e3u9fO1	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: CAT	ECOD (1.6)
P	CAT	e3u9fP1	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: CAT	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
I	3.30.559.10	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Chloramphenicol acetyltransferase-like domain	CATH (4.3.0)
K	3.30.559.10	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Chloramphenicol acetyltransferase-like domain	CATH (4.3.0)
Q [auth R]	3.30.559.10	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Chloramphenicol acetyltransferase-like domain	CATH (4.3.0)
R [auth S]	3.30.559.10	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Chloramphenicol acetyltransferase-like domain	CATH (4.3.0)
A	3.30.559.10	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Chloramphenicol acetyltransferase-like domain	CATH (4.3.0)
B	3.30.559.10	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Chloramphenicol acetyltransferase-like domain	CATH (4.3.0)
C	3.30.559.10	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Chloramphenicol acetyltransferase-like domain	CATH (4.3.0)
D	3.30.559.10	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Chloramphenicol acetyltransferase-like domain	CATH (4.3.0)
E	3.30.559.10	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Chloramphenicol acetyltransferase-like domain	CATH (4.3.0)
F	3.30.559.10	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Chloramphenicol acetyltransferase-like domain	CATH (4.3.0)
G	3.30.559.10	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Chloramphenicol acetyltransferase-like domain	CATH (4.3.0)
H	3.30.559.10	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Chloramphenicol acetyltransferase-like domain	CATH (4.3.0)
J	3.30.559.10	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Chloramphenicol acetyltransferase-like domain	CATH (4.3.0)
L	3.30.559.10	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Chloramphenicol acetyltransferase-like domain	CATH (4.3.0)
M	3.30.559.10	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Chloramphenicol acetyltransferase-like domain	CATH (4.3.0)
N	3.30.559.10	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Chloramphenicol acetyltransferase-like domain	CATH (4.3.0)
O	3.30.559.10	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Chloramphenicol acetyltransferase-like domain	CATH (4.3.0)
P	3.30.559.10	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Chloramphenicol acetyltransferase-like domain	CATH (4.3.0)

AMR Gene: CARD Annotation CARD Database Homepage

Chains	Accession	Short Name	Description	Provenance Source (Version)
A, B, C, D, E, A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q [auth R], R [auth S]	ARO:3002683	catA1	catA1 (formerly in CARD as catI) is a chromosome and transposon-encoded variant of the cat gene found in Escherichia coli and Acinetobacter baumannii.	CARD (3.3.0)

AMR Gene Family: CARD Annotation CARD Database Homepage

Chains	Accession	Gene Family	Drug Class	Resistance Machanism	Provenance Source (Version)
A, B, C, D, E, A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q [auth R], R [auth S]	ARO:3000122	chloramphenicol acetyltransferase (CAT)	phenicol antibiotic	antibiotic inactivation	CARD (3.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E, A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q [auth R], R [auth S]	PF00302	Chloramphenicol acetyltransferase (CAT)	Chloramphenicol acetyltransferase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E, A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q [auth R], R [auth S]	Chloramphenicol acetyltransferase	acetyltransferase activity O-acyltransferase activity acyltransferase activity O-acetyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity catalytic activity chloramphenicol O-acetyltransferase activity	response to stimulus response to chemical response to antibiotic	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E, A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q [auth R], R [auth S]	IPR023213	Chloramphenicol acetyltransferase-like domain superfamily	Homologous Superfamily
A, B, C, D, E, A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q [auth R], R [auth S]	IPR018372	Chloramphenicol acetyltransferase, active site	Active Site
A, B, C, D, E, A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q [auth R], R [auth S]	IPR001707	Chloramphenicol acetyltransferase	Family

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.