6V9Z

Cryo-EM structure of PCAT1 bound to its CtA peptide substrate

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Membrane Protein Annotation: OPM
Membrane Protein Annotation: PDBTM
Membrane Protein Annotation: MemProtMD
Membrane Protein Annotation: mpstruc

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	ABC transporter-like P-loop ATPases	8101175	3002020	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	ABC transporter transmembrane region-like	8101173	3001546	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Cysteine proteinases	8101171	3001808	SCOP2B (2022-06-29)
C [auth B]	SCOP2B Superfamily	ABC transporter-like P-loop ATPases	8101175	3002020	SCOP2B (2022-06-29)
C [auth B]	SCOP2B Superfamily	ABC transporter transmembrane region-like	8101173	3001546	SCOP2B (2022-06-29)
C [auth B]	SCOP2B Superfamily	Cysteine proteinases	8101171	3001808	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)
A	PF00664	e6v9zA2	A: alpha bundles	X: Type II ABC exporter transmembrane domain fold	H: Type I ABC exporter transmembrane domain fold (From Topology)	T: Type I ABC exporter transmembrane domain fold	F: PF00664	ECOD (1.6)
A	PF03412	e6v9zA1	A: a+b complex topology	X: Cysteine proteinases-like	H: Cysteine proteinases (From Topology)	T: Cysteine proteinases	F: PF03412	ECOD (1.6)
A	PF00005	e6v9zA3	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: PF00005	ECOD (1.6)
C [auth B]	PF00664	e6v9zB1	A: alpha bundles	X: Type II ABC exporter transmembrane domain fold	H: Type I ABC exporter transmembrane domain fold (From Topology)	T: Type I ABC exporter transmembrane domain fold	F: PF00664	ECOD (1.6)
C [auth B]	PF03412	e6v9zB2	A: a+b complex topology	X: Cysteine proteinases-like	H: Cysteine proteinases (From Topology)	T: Cysteine proteinases	F: PF03412	ECOD (1.6)
C [auth B]	PF00005	e6v9zB3	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: PF00005	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.70.10	Alpha Beta	Alpha-Beta Complex	Cathepsin B	Chain A	CATH (utative)
A	1.20.1560.10	Mainly Alpha	Up-down Bundle	ABC transporter transmembrane region fold	ABC transporter type 1, transmembrane domain	CATH (utative)
A	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (utative)
C [auth B]	3.90.70.10	Alpha Beta	Alpha-Beta Complex	Cathepsin B	Chain A	CATH (utative)
C [auth B]	1.20.1560.10	Mainly Alpha	Up-down Bundle	ABC transporter transmembrane region fold	ABC transporter type 1, transmembrane domain	CATH (utative)
C [auth B]	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, C [auth B]	PF03412	Peptidase C39 family (Peptidase_C39)	Peptidase C39 family	-	Family
A, C [auth B]	PF00664	ABC transporter transmembrane region (ABC_membrane)	ABC transporter transmembrane region	-	Family
A, C [auth B]	PF00005	ABC transporter (ABC_tran)	ABC transporter	ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are comp ...	ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain Pfam:PF00664. These four domains may belong to a single polypeptide as in Swiss:P13569, or belong in different polypeptide chains.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, C [auth B]	ABC-type bacteriocin transporter	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding primary active transmembrane transporter activity ATPase-coupled transmembrane transporter activity amide transmembrane transporter activity ATP-dependent activity xenobiotic transmembrane transporter activity ABC-type transporter activity active transmembrane transporter activity ABC-type xenobiotic transporter activity transporter activity ABC-type bacteriocin transporter activity transmembrane transporter activity bacteriocin transmembrane transporter activity pyrophosphatase activity ATP hydrolysis activity ribonucleoside triphosphate phosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity hydrolase activity, acting on acid anhydrides catalytic activity cysteine-type peptidase activity peptidase activity catalytic activity, acting on a protein	organic substance metabolic process organonitrogen compound metabolic process proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process	membrane cellular anatomical entity
B [auth C], D	CtA	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, C [auth B]	IPR005897	Peptidase C39, ABC-type bacteriocin transporter	Family
A, C [auth B]	IPR005074	Peptidase C39, bacteriocin processing	Domain
A, C [auth B]	IPR003439	ABC transporter-like, ATP-binding domain	Domain
A, C [auth B]	IPR036640	ABC transporter type 1, transmembrane domain superfamily	Homologous Superfamily
A, C [auth B]	IPR003593	AAA+ ATPase domain	Domain
A, C [auth B]	IPR011527	ABC transporter type 1, transmembrane domain	Domain
A, C [auth B]	IPR039421	Type 1 protein exporter	Family
A, C [auth B]	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A, C [auth B]	OPM	Transmembrane	Alpha-helical polytopic	ABC transporters	Lipid exporter family

Membrane Protein Annotation: PDBTM PDBTM Database Homepage

Chains	External Link	Comment
A, C [auth B]	PDBTM	Annotated as membrane protein by PDBTM

Membrane Protein Annotation: MemProtMD MemProtMD Database Homepage

Chains	External Link	Comment
A, C [auth B]	MemProtMD	Annotated as membrane protein by MemProtMD

Membrane Protein Annotation: mpstruc mpstruc Database Homepage

Chains	Resource Link	Group	Subgroup	Protein
A, C [auth B]	mpstruc	TRANSMEMBRANE PROTEINS: ALPHA-HELICAL	ATP Binding Cassette (ABC) Transporters	Peptidase-containing ABC transporter (PCAT1) bound to CtA peptide substrate

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 R01GM133198.