Annotations: 1J2T

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1j2ta_	Alpha and beta proteins (a/b)	Creatininase	Creatininase	Creatininase	Creatininase	(Pseudomonas putida ) [TaxId: 303 ],	SCOPe (2.08)
B	d1j2tb_	Alpha and beta proteins (a/b)	Creatininase	Creatininase	Creatininase	Creatininase	(Pseudomonas putida ) [TaxId: 303 ],	SCOPe (2.08)
C	d1j2tc_	Alpha and beta proteins (a/b)	Creatininase	Creatininase	Creatininase	Creatininase	(Pseudomonas putida ) [TaxId: 303 ],	SCOPe (2.08)
D	d1j2td_	Alpha and beta proteins (a/b)	Creatininase	Creatininase	Creatininase	Creatininase	(Pseudomonas putida ) [TaxId: 303 ],	SCOPe (2.08)
E	d1j2te_	Alpha and beta proteins (a/b)	Creatininase	Creatininase	Creatininase	Creatininase	(Pseudomonas putida ) [TaxId: 303 ],	SCOPe (2.08)
F	d1j2tf_	Alpha and beta proteins (a/b)	Creatininase	Creatininase	Creatininase	Creatininase	(Pseudomonas putida ) [TaxId: 303 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Creatininase	8035599	3000410	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Creatininase	8035599	3000410	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Creatininase	8035599	3000410	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Creatininase	8035599	3000410	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Creatininase	8035599	3000410	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Creatininase	8035599	3000410	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	Creatininase	e1j2tA1	A: a/b three-layered sandwiches	X: Creatininase (From Topology)	H: Creatininase (From Topology)	T: Creatininase	F: Creatininase	ECOD (1.6)
B	Creatininase	e1j2tB1	A: a/b three-layered sandwiches	X: Creatininase (From Topology)	H: Creatininase (From Topology)	T: Creatininase	F: Creatininase	ECOD (1.6)
C	Creatininase	e1j2tC1	A: a/b three-layered sandwiches	X: Creatininase (From Topology)	H: Creatininase (From Topology)	T: Creatininase	F: Creatininase	ECOD (1.6)
D	Creatininase	e1j2tD1	A: a/b three-layered sandwiches	X: Creatininase (From Topology)	H: Creatininase (From Topology)	T: Creatininase	F: Creatininase	ECOD (1.6)
E	Creatininase	e1j2tE1	A: a/b three-layered sandwiches	X: Creatininase (From Topology)	H: Creatininase (From Topology)	T: Creatininase	F: Creatininase	ECOD (1.6)
F	Creatininase	e1j2tF1	A: a/b three-layered sandwiches	X: Creatininase (From Topology)	H: Creatininase (From Topology)	T: Creatininase	F: Creatininase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.10310	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Creatininase	CATH (4.3.0)
B	3.40.50.10310	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Creatininase	CATH (4.3.0)
C	3.40.50.10310	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Creatininase	CATH (4.3.0)
D	3.40.50.10310	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Creatininase	CATH (4.3.0)
E	3.40.50.10310	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Creatininase	CATH (4.3.0)
F	3.40.50.10310	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Creatininase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	PF02633	Creatinine amidohydrolase (Creatininase)	Creatinine amidohydrolase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	creatinine amidohydrolase	cation binding manganese ion binding transition metal ion binding ion binding binding metal ion binding small molecule binding hydrolase activity creatininase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds zinc ion binding	organonitrogen compound catabolic process creatinine metabolic process catabolic process organonitrogen compound metabolic process creatinine catabolic process lactam catabolic process organic cyclic compound catabolic process lactam metabolic process organic cyclic compound metabolic process organic substance metabolic process metabolic process small molecule metabolic process amide metabolic process organic substance catabolic process organonitrogen compound catabolic process creatinine metabolic process catabolic process organonitrogen compound metabolic process creatinine catabolic process lactam catabolic process organic cyclic compound catabolic process lactam metabolic process organic cyclic compound metabolic process organic substance metabolic process metabolic process small molecule metabolic process amide metabolic process organic substance catabolic process monocarboxylic acid biosynthetic process creatine metabolic process small molecule biosynthetic process oxoacid metabolic process cellular biosynthetic process creatine biosynthetic process cellular metabolic process organonitrogen compound biosynthetic process carboxylic acid metabolic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process cellular modified amino acid metabolic process biosynthetic process cellular modified amino acid biosynthetic process organic substance biosynthetic process cellular process monocarboxylic acid metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR003785	Creatininase/formamide hydrolase	Family
A, B, C, D, E A, B, C, D, E, F	IPR024087	Creatininase-like superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR031034	Creatinine amidohydrolase	Family

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.