1Z2L

Crystal structure of Allantoate-amidohydrolase from E.coli K12 in complex with substrate Allantoate

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	d1z2la1	Alpha and beta proteins (a/b)	Phosphorylase/hydrolase-like	Zn-dependent exopeptidases	Bacterial dinuclear zinc exopeptidases	Allantoate amidohydrolase AllC catalytic domain	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
A	d1z2la2	Alpha and beta proteins (a+b)	Ferredoxin-like	Bacterial exopeptidase dimerisation domain	Bacterial exopeptidase dimerisation domain	Allantoate amidohydrolase AllC	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
A	d1z2la3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
B	d1z2lb1	Alpha and beta proteins (a/b)	Phosphorylase/hydrolase-like	Zn-dependent exopeptidases	Bacterial dinuclear zinc exopeptidases	Allantoate amidohydrolase AllC catalytic domain	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
B	d1z2lb2	Alpha and beta proteins (a+b)	Ferredoxin-like	Bacterial exopeptidase dimerisation domain	Bacterial exopeptidase dimerisation domain	Allantoate amidohydrolase AllC	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
B	d1z2lb3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli K-12 ) [TaxId: 83333 ],	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 dinuclear zinc exopeptidases	8022730	4000587	SCOP2 (2022-06-29)
A	SCOP2 Family	Bacterial exopeptidase dimerisation domain	8022731	4001271	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Zn-dependent exopeptidases	8035110	3000662	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Bacterial exopeptidase dimerisation domain	8035111	3001194	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Zn-dependent exopeptidases	8035110	3000662	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Bacterial exopeptidase dimerisation domain	8035111	3001194	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Zn-dependent exopeptidases	8035110	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	M20_dimer_1	e1z2lA1	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	e1z2lA2	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	e1z2lB1	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	e1z2lB2	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	Allantoate amidohydrolase	cation binding manganese ion binding transition metal ion binding ion binding binding metal ion binding small molecule binding identical protein binding protein binding protein homodimerization activity protein dimerization activity zinc ion binding allantoate deiminase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines cation binding manganese ion binding transition metal ion binding ion binding binding metal ion binding small molecule binding identical protein binding protein binding protein homodimerization activity protein dimerization activity zinc ion binding allantoate deiminase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines hydrolase activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds	allantoin metabolic process catabolic process amide catabolic process metabolic process amide metabolic process allantoin assimilation pathway allantoin catabolic process nucleobase-containing compound metabolic process purine nucleobase metabolic process nucleobase-containing small molecule metabolic process nucleobase metabolic process small molecule metabolic process primary metabolic process purine-containing compound metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity

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	IPR017591	Allantoate amidohydrolase	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.