2BTW

Crystal structure of Alr0975

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
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	d2btwa1	Alpha and beta proteins (a+b)	Cysteine proteinases	Cysteine proteinases	Phytochelatin synthase	Primitive phytochelatin synthase	NOSTOC SP. PCC 7120 (Nostoc sp. PCC 7120 = FACHB-418 ) [TaxId: 103690 ],	SCOPe (2.08)
B	d2btwb1	Alpha and beta proteins (a+b)	Cysteine proteinases	Cysteine proteinases	Phytochelatin synthase	Primitive phytochelatin synthase	NOSTOC SP. PCC 7120 (Nostoc sp. PCC 7120 = FACHB-418 ) [TaxId: 103690 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Cysteine proteinases	8038611	3001808	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Cysteine proteinases	8038611	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	Phytochelatin	e2btwA1	A: a+b complex topology	X: Cysteine proteinases-like	H: Cysteine proteinases (From Topology)	T: Cysteine proteinases	F: Phytochelatin	ECOD (1.6)
B	Phytochelatin	e2btwB1	A: a+b complex topology	X: Cysteine proteinases-like	H: Cysteine proteinases (From Topology)	T: Cysteine proteinases	F: Phytochelatin	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.70.30	Alpha Beta	Alpha-Beta Complex	Cathepsin B	Chain A	CATH (4.3.0)
B	3.90.70.30	Alpha Beta	Alpha-Beta Complex	Cathepsin B	Chain A	CATH (4.3.0)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	ALR0975 PROTEIN	aminoacyltransferase activity glutathione gamma-glutamylcysteinyltransferase activity acyltransferase activity transferase activity catalytic activity cation binding ion binding binding metal ion binding small molecule binding	response to stimulus response to metal ion response to chemical biosynthetic process secondary metabolite biosynthetic process phytochelatin biosynthetic process amide biosynthetic process metabolic process amide metabolic process phytochelatin metabolic process secondary metabolic process	-
B	ALR0975 PROTEIN	aminoacyltransferase activity glutathione gamma-glutamylcysteinyltransferase activity acyltransferase activity transferase activity catalytic activity cation binding ion binding binding metal ion binding small molecule binding	response to stimulus response to metal ion response to chemical biosynthetic process secondary metabolite biosynthetic process phytochelatin biosynthetic process amide biosynthetic process metabolic process amide metabolic process phytochelatin metabolic process secondary metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR007719	Phytochelatin synthase, N-terminal catalytic domain	Domain
A	IPR038156	Phytochelatin synthase, N-terminal domain superfamily	Homologous Superfamily
A	IPR038765	Papain-like cysteine peptidase superfamily	Homologous Superfamily
A	IPR040409	Phytochelatin synthase	Family
B	IPR007719	Phytochelatin synthase, N-terminal catalytic domain	Domain
B	IPR038156	Phytochelatin synthase, N-terminal domain superfamily	Homologous Superfamily
B	IPR038765	Papain-like cysteine peptidase superfamily	Homologous Superfamily
B	IPR040409	Phytochelatin synthase	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.