5WIF

Crystal structure of spermidine/spermine N-acetyltransferase SpeG from Yersinia pestis

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
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)
A	d5wifa_	Alpha and beta proteins (a+b)	Acyl-CoA N-acyltransferases (Nat)	Acyl-CoA N-acyltransferases (Nat)	automated matches	automated matches	(Yersinia pestis ) [TaxId: 632 ],	SCOPe (2.08)
B	d5wifb1	Alpha and beta proteins (a+b)	Acyl-CoA N-acyltransferases (Nat)	Acyl-CoA N-acyltransferases (Nat)	automated matches	automated matches	(Yersinia pestis ) [TaxId: 632 ],	SCOPe (2.08)
B	d5wifb2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Yersinia pestis ) [TaxId: 632 ],	SCOPe (2.08)
C	d5wifc1	Alpha and beta proteins (a+b)	Acyl-CoA N-acyltransferases (Nat)	Acyl-CoA N-acyltransferases (Nat)	automated matches	automated matches	(Yersinia pestis ) [TaxId: 632 ],	SCOPe (2.08)
C	d5wifc2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Yersinia pestis ) [TaxId: 632 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Acyl-CoA N-acyltransferases (Nat)	8060303	3000403	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Acyl-CoA N-acyltransferases (Nat)	8060303	3000403	SCOP2B (2022-06-29)
C	SCOP2 Family	N-acetyltransferase, NAT	8060302	4001800	SCOP2 (2022-06-29)
C	SCOP2 Superfamily	Acyl-CoA N-acyltransferases (Nat)	8060303	3000403	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Acetyltransf_3_1	e5wifA1	A: a+b three layers	X: Nat/Ivy	H: Acyl-CoA N-acyltransferases (Nat) (From Topology)	T: Acyl-CoA N-acyltransferases (Nat)	F: Acetyltransf_3_1	ECOD (1.6)
B	Acetyltransf_3_1	e5wifB1	A: a+b three layers	X: Nat/Ivy	H: Acyl-CoA N-acyltransferases (Nat) (From Topology)	T: Acyl-CoA N-acyltransferases (Nat)	F: Acetyltransf_3_1	ECOD (1.6)
C	Acetyltransf_3_1	e5wifC1	A: a+b three layers	X: Nat/Ivy	H: Acyl-CoA N-acyltransferases (Nat) (From Topology)	T: Acyl-CoA N-acyltransferases (Nat)	F: Acetyltransf_3_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.630.30	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Gcn5-related N-acetyltransferase (GNAT)	CATH (4.3.0)
B	3.40.630.30	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Gcn5-related N-acetyltransferase (GNAT)	CATH (4.3.0)
C	3.40.630.30	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Gcn5-related N-acetyltransferase (GNAT)	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF13302	Acetyltransferase (GNAT) domain (Acetyltransf_3)	Acetyltransferase (GNAT) domain	This domain catalyses N-acetyltransferase reactions.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	Spermidine N1-acetyltransferase	acetyltransferase activity N-acetyltransferase activity acyltransferase activity diamine N-acetyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity catalytic activity N-acyltransferase activity cation binding ion binding binding metal ion binding small molecule binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR016181	Acyl-CoA N-acyltransferase	Homologous Superfamily
A, B, C	IPR000182	GNAT domain	Domain

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.