Annotations: 1CG2

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1cg2a1	Alpha and beta proteins (a/b)	Phosphorylase/hydrolase-like	Zn-dependent exopeptidases	Bacterial dinuclear zinc exopeptidases	Carboxypeptidase G2, catalytic domain	(Pseudomonas sp. RS-16 ) [TaxId: 312 ],	SCOPe (2.08)
A	d1cg2a2	Alpha and beta proteins (a+b)	Ferredoxin-like	Bacterial exopeptidase dimerisation domain	Bacterial exopeptidase dimerisation domain	Carboxypeptidase G2	(Pseudomonas sp. RS-16 ) [TaxId: 312 ],	SCOPe (2.08)
B	d1cg2b1	Alpha and beta proteins (a/b)	Phosphorylase/hydrolase-like	Zn-dependent exopeptidases	Bacterial dinuclear zinc exopeptidases	Carboxypeptidase G2, catalytic domain	(Pseudomonas sp. RS-16 ) [TaxId: 312 ],	SCOPe (2.08)
B	d1cg2b2	Alpha and beta proteins (a+b)	Ferredoxin-like	Bacterial exopeptidase dimerisation domain	Bacterial exopeptidase dimerisation domain	Carboxypeptidase G2	(Pseudomonas sp. RS-16 ) [TaxId: 312 ],	SCOPe (2.08)
C	d1cg2c1	Alpha and beta proteins (a/b)	Phosphorylase/hydrolase-like	Zn-dependent exopeptidases	Bacterial dinuclear zinc exopeptidases	Carboxypeptidase G2, catalytic domain	(Pseudomonas sp. RS-16 ) [TaxId: 312 ],	SCOPe (2.08)
C	d1cg2c2	Alpha and beta proteins (a+b)	Ferredoxin-like	Bacterial exopeptidase dimerisation domain	Bacterial exopeptidase dimerisation domain	Carboxypeptidase G2	(Pseudomonas sp. RS-16 ) [TaxId: 312 ],	SCOPe (2.08)
D	d1cg2d1	Alpha and beta proteins (a/b)	Phosphorylase/hydrolase-like	Zn-dependent exopeptidases	Bacterial dinuclear zinc exopeptidases	Carboxypeptidase G2, catalytic domain	(Pseudomonas sp. RS-16 ) [TaxId: 312 ],	SCOPe (2.08)
D	d1cg2d2	Alpha and beta proteins (a+b)	Ferredoxin-like	Bacterial exopeptidase dimerisation domain	Bacterial exopeptidase dimerisation domain	Carboxypeptidase G2	(Pseudomonas sp. RS-16 ) [TaxId: 312 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Bacterial exopeptidase dimerisation domain	8023136	4001271	SCOP2 (2022-06-29)
A	SCOP2 Family	Bacterial dinuclear zinc exopeptidases	8019823	4000587	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Bacterial exopeptidase dimerisation domain	8035516	3001194	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Zn-dependent exopeptidases	8032203	3000662	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Bacterial exopeptidase dimerisation domain	8035516	3001194	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Zn-dependent exopeptidases	8032203	3000662	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Zn-dependent exopeptidases	8032203	3000662	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Zn-dependent exopeptidases	8032203	3000662	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Bacterial exopeptidase dimerisation domain	8035516	3001194	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Zn-dependent exopeptidases	8032203	3000662	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Bacterial exopeptidase dimerisation domain	8035516	3001194	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Zn-dependent exopeptidases	8032203	3000662	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Zn-dependent exopeptidases	8032203	3000662	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	PF07687	e1cg2A1	A: a+b two layers	X: Alpha-beta plaits	H: Bacterial exopeptidase dimerisation domain (From Topology)	T: Bacterial exopeptidase dimerisation domain	F: PF07687	ECOD (1.6)
A	PF01546	e1cg2A2	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Zn-dependent exopeptidases (From Topology)	T: Zn-dependent exopeptidases	F: PF01546	ECOD (1.6)
B	PF07687	e1cg2B1	A: a+b two layers	X: Alpha-beta plaits	H: Bacterial exopeptidase dimerisation domain (From Topology)	T: Bacterial exopeptidase dimerisation domain	F: PF07687	ECOD (1.6)
B	PF01546	e1cg2B2	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Zn-dependent exopeptidases (From Topology)	T: Zn-dependent exopeptidases	F: PF01546	ECOD (1.6)
C	PF07687	e1cg2C1	A: a+b two layers	X: Alpha-beta plaits	H: Bacterial exopeptidase dimerisation domain (From Topology)	T: Bacterial exopeptidase dimerisation domain	F: PF07687	ECOD (1.6)
C	PF01546	e1cg2C2	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Zn-dependent exopeptidases (From Topology)	T: Zn-dependent exopeptidases	F: PF01546	ECOD (1.6)
D	PF07687	e1cg2D1	A: a+b two layers	X: Alpha-beta plaits	H: Bacterial exopeptidase dimerisation domain (From Topology)	T: Bacterial exopeptidase dimerisation domain	F: PF07687	ECOD (1.6)
D	PF01546	e1cg2D2	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Zn-dependent exopeptidases (From Topology)	T: Zn-dependent exopeptidases	F: PF01546	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.630.10	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Zn peptidases	CATH (4.3.0)
A	3.30.70.360	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)
B	3.40.630.10	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Zn peptidases	CATH (4.3.0)
B	3.30.70.360	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)
C	3.40.630.10	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Zn peptidases	CATH (4.3.0)
C	3.30.70.360	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)
D	3.40.630.10	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Zn peptidases	CATH (4.3.0)
D	3.30.70.360	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF01546	Peptidase family M20/M25/M40 (Peptidase_M20)	Peptidase family M20/M25/M40	-	Family
A, B, C, D	PF07687	Peptidase dimerisation domain (M20_dimer)	Peptidase dimerisation domain	This domain consists of 4 beta strands and two alpha helices which make up the dimerisation surface of members of the M20 family of peptidases [1]. This family includes a range of zinc metallopeptidases belonging to several families in the peptidase ...	This domain consists of 4 beta strands and two alpha helices which make up the dimerisation surface of members of the M20 family of peptidases [1]. This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification [2]. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	CARBOXYPEPTIDASE G2	peptidase activity catalytic activity, acting on a protein metallopeptidase activity hydrolase activity catalytic activity exopeptidase activity carboxypeptidase activity cation binding ion binding binding metal ion binding small molecule binding	organic substance metabolic process organonitrogen compound metabolic process proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR017150	Peptidase M20, glutamate carboxypeptidase	Family
A, B, C, D	IPR002933	Peptidase M20	Family
A, B, C, D	IPR001261	ArgE/DapE/ACY1/CPG2/YscS, conserved site	Conserved Site
A, B, C, D	IPR036264	Bacterial exopeptidase dimerisation domain	Homologous Superfamily
A, B, C, D	IPR011650	Peptidase M20, dimerisation domain	Domain

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	glutamate carboxypeptidase M-CSA #447	Glutamate carboxypeptidase (also known as carboxypeptidase G2, CPDG2, CPG2 or folate hydrolase G2) belongs to the peptidase M20A family. G2 is a periplasmic enzyme that is synthesized with a signal peptide and is a dimeric zinc-dependent exopeptidase, with two domains, a catalytic domain, which provides the ligands for the two zinc ions in the active site, and a dimerization domain. It is known to cleave the C-terminal glutamate moiety from a wide range of N-acyl groups, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl (shown in the reference reaction), and pteroyl groups to release benzoic acid, phenol, and aniline mustards. It is used clinically to treat methotrexate toxicity by hydrolysing methotrexate to inactive and non-toxic metabolites. It is also proposed for use in antibody-directed enzyme prodrug therapy against tumor cells.	Defined by 6 residues: HIS:A-90 [auth A-112]ASP:A-119 [auth A-141]GLU:A-153 [auth A-175]GLU:A-154 [auth A-176]GLU:A-178 [auth A-200]HIS:A-363 [auth A-385] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.4.17.11 (PDB Primary Data) Search M-CSA Motif + EC 3.4.17.11

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.