Annotations: 5WZE

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d5wzea1	Alpha and beta proteins (a/b)	Ribonuclease H-like motif	Creatinase/prolidase N-terminal domain	automated matches	automated matches	(Pseudomonas aeruginosa PAO1 ) [TaxId: 208964 ],	SCOPe (2.08)
A	d5wzea2	Alpha and beta proteins (a+b)	Creatinase/aminopeptidase	Creatinase/aminopeptidase	automated matches	automated matches	(Pseudomonas aeruginosa PAO1 ) [TaxId: 208964 ],	SCOPe (2.08)
C	d5wzec1	Alpha and beta proteins (a/b)	Ribonuclease H-like motif	Creatinase/prolidase N-terminal domain	automated matches	automated matches	(Pseudomonas aeruginosa PAO1 ) [TaxId: 208964 ],	SCOPe (2.08)
C	d5wzec2	Alpha and beta proteins (a+b)	Creatinase/aminopeptidase	Creatinase/aminopeptidase	automated matches	automated matches	(Pseudomonas aeruginosa PAO1 ) [TaxId: 208964 ],	SCOPe (2.08)
D	d5wzed1	Alpha and beta proteins (a/b)	Ribonuclease H-like motif	Creatinase/prolidase N-terminal domain	automated matches	automated matches	(Pseudomonas aeruginosa PAO1 ) [TaxId: 208964 ],	SCOPe (2.08)
D	d5wzed2	Alpha and beta proteins (a+b)	Creatinase/aminopeptidase	Creatinase/aminopeptidase	automated matches	automated matches	(Pseudomonas aeruginosa PAO1 ) [TaxId: 208964 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF00557	e5wzeA1	A: a+b duplicates or obligate multimers	X: Creatinase/aminopeptidase-like	H: Creatinase/aminopeptidase (From Topology)	T: Creatinase/aminopeptidase	F: PF00557	ECOD (1.6)
A	PF05195	e5wzeA2	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Creatinase/prolidase N-terminal domain (From Topology)	T: Creatinase/prolidase N-terminal domain	F: PF05195	ECOD (1.6)
B	PF00557	e5wzeB1	A: a+b duplicates or obligate multimers	X: Creatinase/aminopeptidase-like	H: Creatinase/aminopeptidase (From Topology)	T: Creatinase/aminopeptidase	F: PF00557	ECOD (1.6)
B	PF05195	e5wzeB2	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Creatinase/prolidase N-terminal domain (From Topology)	T: Creatinase/prolidase N-terminal domain	F: PF05195	ECOD (1.6)
C	PF00557	e5wzeC2	A: a+b duplicates or obligate multimers	X: Creatinase/aminopeptidase-like	H: Creatinase/aminopeptidase (From Topology)	T: Creatinase/aminopeptidase	F: PF00557	ECOD (1.6)
C	PF05195	e5wzeC1	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Creatinase/prolidase N-terminal domain (From Topology)	T: Creatinase/prolidase N-terminal domain	F: PF05195	ECOD (1.6)
D	PF00557	e5wzeD1	A: a+b duplicates or obligate multimers	X: Creatinase/aminopeptidase-like	H: Creatinase/aminopeptidase (From Topology)	T: Creatinase/aminopeptidase	F: PF00557	ECOD (1.6)
D	PF05195	e5wzeD2	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Creatinase/prolidase N-terminal domain (From Topology)	T: Creatinase/prolidase N-terminal domain	F: PF05195	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.350.10	Alpha Beta	3-Layer(aba) Sandwich	Creatine Amidinohydrolase	Chain A, domain 1	CATH (4.3.0)
A	3.90.230.10	Alpha Beta	Alpha-Beta Complex	Creatine Amidinohydrolase	Creatinase/methionine aminopeptidase superfamily	CATH (4.3.0)
B	3.40.350.10	Alpha Beta	3-Layer(aba) Sandwich	Creatine Amidinohydrolase	Chain A, domain 1	CATH (4.3.0)
B	3.90.230.10	Alpha Beta	Alpha-Beta Complex	Creatine Amidinohydrolase	Creatinase/methionine aminopeptidase superfamily	CATH (4.3.0)
C	3.40.350.10	Alpha Beta	3-Layer(aba) Sandwich	Creatine Amidinohydrolase	Chain A, domain 1	CATH (4.3.0)
C	3.90.230.10	Alpha Beta	Alpha-Beta Complex	Creatine Amidinohydrolase	Creatinase/methionine aminopeptidase superfamily	CATH (4.3.0)
D	3.40.350.10	Alpha Beta	3-Layer(aba) Sandwich	Creatine Amidinohydrolase	Chain A, domain 1	CATH (4.3.0)
D	3.90.230.10	Alpha Beta	Alpha-Beta Complex	Creatine Amidinohydrolase	Creatinase/methionine aminopeptidase superfamily	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF05195	Aminopeptidase P, N-terminal domain (AMP_N)	Aminopeptidase P, N-terminal domain	This domain is structurally very similar [1] to the creatinase N-terminal domain (Pfam:PF01321). However, little or no sequence similarity exists between the two families.	Domain
A, B, C, D	PF00557	Metallopeptidase family M24 (Peptidase_M24)	Metallopeptidase family M24	This family contains metallopeptidases. It also contains non-peptidase homologues such as the N terminal domain of Spt16 which is a histone H3-H4 binding module [3].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Aminopeptidase P	cation binding manganese ion binding transition metal ion binding ion binding binding metal ion binding small molecule binding peptidase activity catalytic activity, acting on a protein hydrolase activity metallopeptidase activity aminopeptidase activity metalloaminopeptidase activity exopeptidase activity cation binding manganese ion binding transition metal ion binding ion binding binding metal ion binding small molecule binding peptidase activity catalytic activity, acting on a protein hydrolase activity metallopeptidase activity aminopeptidase activity metalloaminopeptidase activity exopeptidase activity catalytic activity metalloexopeptidase activity	organic substance metabolic process organonitrogen compound metabolic process proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR007865	Aminopeptidase P, N-terminal	Domain
A, B, C, D	IPR029149	Creatinase/Aminopeptidase P/Spt16, N-terminal	Homologous Superfamily
A, B, C, D	IPR036005	Creatinase/aminopeptidase-like	Homologous Superfamily
A, B, C, D	IPR000994	Peptidase M24	Domain

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.