Annotations: 4PXC

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	M20_dimer_1	e4pxcA2	A: a+b two layers	X: Alpha-beta plaits	H: Bacterial exopeptidase dimerisation domain (From Topology)	T: Bacterial exopeptidase dimerisation domain	F: M20_dimer_1	ECOD (1.6)
A	Peptidase_M28	e4pxcA1	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Zn-dependent exopeptidases (From Topology)	T: Zn-dependent exopeptidases	F: Peptidase_M28	ECOD (1.6)
B	M20_dimer_1	e4pxcB2	A: a+b two layers	X: Alpha-beta plaits	H: Bacterial exopeptidase dimerisation domain (From Topology)	T: Bacterial exopeptidase dimerisation domain	F: M20_dimer_1	ECOD (1.6)
B	Peptidase_M28	e4pxcB1	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Zn-dependent exopeptidases (From Topology)	T: Zn-dependent exopeptidases	F: Peptidase_M28	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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF01546	Peptidase family M20/M25/M40 (Peptidase_M20)	Peptidase family M20/M25/M40	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Ureidoglycolate hydrolase	cation binding manganese ion binding transition metal ion binding ion binding binding metal ion binding small molecule binding ureidoglycolate hydrolase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides hydrolase activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines	catabolic process purine nucleobase metabolic process primary metabolic process purine-containing compound catabolic process purine nucleobase catabolic process purine-containing compound metabolic process nucleobase-containing compound metabolic process nucleobase catabolic process nucleobase-containing small molecule metabolic process nucleobase metabolic process small molecule metabolic process metabolic process ureide metabolic process amide metabolic process catabolic process purine nucleobase metabolic process primary metabolic process purine-containing compound catabolic process purine nucleobase catabolic process purine-containing compound metabolic process nucleobase-containing compound metabolic process nucleobase catabolic process nucleobase-containing small molecule metabolic process nucleobase metabolic process small molecule metabolic process metabolic process ureide metabolic process amide metabolic process ureide catabolic process allantoin metabolic process amide catabolic process allantoin catabolic process	membrane-bounded organelle intracellular organelle intracellular anatomical structure plastid organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle endoplasmic reticulum endomembrane system

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR002933	Peptidase M20	Family
A, B	IPR010158	Amidase, carbamoylase-type	Family
A, B	IPR036264	Bacterial exopeptidase dimerisation domain	Homologous Superfamily

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.