5JR6

The Xray Crystal Structure of P. falciparum Aminopeptidase P in Complex With Apstatin

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Protein Modification Annotation

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Creatinase/aminopeptidase-like	8054225	4000207	SCOP2 (2022-06-29)
A	SCOP2 Family	Cytosolic X-prolyl aminopeptidase domain 2-like	8045060	4004281	SCOP2 (2022-06-29)
A	SCOP2 Family	Creatinase/prolidase N-terminal domain	8054223	4000535	SCOP2 (2022-06-29)
A	SCOP2 Family	Peptidase M24 C-terminal domain-like	8045051	4004278	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Creatinase/aminopeptidase catalytic domain-like	8054226	3000126	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Creatinase/prolidase N-terminal domain-like	8054222	3000538	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Creatinase/prolidase N-terminal domain-like	8054224	3000538	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Peptidase M24 C-terminal domain-like	8054221	3002284	SCOP2 (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	Peptidase_M24	e5jr6A3	A: a+b duplicates or obligate multimers	X: Creatinase/aminopeptidase-like	H: Creatinase/aminopeptidase (From Topology)	T: Creatinase/aminopeptidase	F: Peptidase_M24	ECOD (1.6)
A	Creatinase_N	e5jr6A2	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: Creatinase_N	ECOD (1.6)
A	Creatinase_N_2	e5jr6A1	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: Creatinase_N_2	ECOD (1.6)
B	Peptidase_M24	e5jr6B1	A: a+b duplicates or obligate multimers	X: Creatinase/aminopeptidase-like	H: Creatinase/aminopeptidase (From Topology)	T: Creatinase/aminopeptidase	F: Peptidase_M24	ECOD (1.6)
B	Creatinase_N	e5jr6B3	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: Creatinase_N	ECOD (1.6)
B	Creatinase_N_2	e5jr6B2	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: Creatinase_N_2	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	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	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
A, B	PF16188	C-terminal region of peptidase_M24 (Peptidase_M24_C)	C-terminal region of peptidase_M24	This is a short region at the C-terminus of a number of metallo-peptidases of the M24 family.	Domain
A, B	PF01321	Creatinase/Prolidase N-terminal domain (Creatinase_N)	Creatinase/Prolidase N-terminal domain	This family includes the N-terminal non-catalytic domains from creatinase and prolidase. The exact function of this domain is uncertain.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Peptidase, putative	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	organonitrogen compound catabolic process organonitrogen compound metabolic process catabolic process primary metabolic process protein catabolic process macromolecule catabolic process hemoglobin catabolic process organic substance metabolic process metabolic process protein metabolic process macromolecule metabolic process organic substance catabolic process hemoglobin metabolic process proteolysis	intracellular anatomical structure cytoplasm cellular anatomical entity membrane-bounded organelle phagolysosome lytic vacuole intracellular vesicle vacuole phagocytic vesicle intracellular membrane-bounded organelle food vacuole intracellular organelle cytoplasmic vesicle organelle intracellular anatomical structure cytoplasm cellular anatomical entity membrane-bounded organelle phagolysosome lytic vacuole intracellular vesicle vacuole phagocytic vesicle intracellular membrane-bounded organelle food vacuole intracellular organelle cytoplasmic vesicle organelle secondary lysosome vesicle endocytic vesicle lysosome membrane-enclosed lumen vacuolar lumen intracellular organelle lumen organelle lumen
C [auth F]	Apstatin	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR001131	Peptidase M24B, X-Pro dipeptidase/aminopeptidase P, conserved site	Conserved Site
A, B	IPR000587	Creatinase, N-terminal	Domain
A, B	IPR029149	Creatinase/Aminopeptidase P/Spt16, N-terminal	Homologous Superfamily
A, B	IPR033740	Aminopeptidase P	Domain
A, B	IPR032416	Peptidase M24, C-terminal domain	Domain
A, B	IPR036005	Creatinase/aminopeptidase-like	Homologous Superfamily
A, B	IPR000994	Peptidase M24	Domain

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
C [auth F]	01B
C [auth F]	NH2	RESID: AA0081 , AA0083 , AA0084 , AA0086 , AA0087 , AA0088 , AA0090 , AA0091 , AA0092 , AA0093 , AA0095 , AA0096 , AA0097 , AA0098 , AA0099 , AA0100 PSI-MOD : L-alanine amide MOD:00090 , L-asparagine amide MOD:00092 , L-aspartic acid 1-amide MOD:00093 , L-glutamine amide MOD:00095 , L-glutamic acid 1-amide MOD:00096 , glycine amide MOD:00097 , L-isoleucine amide MOD:00099 , L-leucine amide MOD:00100 , L-lysine amide MOD:00101 , L-methionine amide MOD:00102 , L-proline amide MOD:00104 , L-serine amide MOD:00105 , L-threonine amide MOD:00106 , L-tryptophan amide MOD:00107 , L-tyrosine amide MOD:00108 , L-valine amide MOD:00109

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.