5AB0

Crystal structure of aminopeptidase ERAP2 with ligand

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
Pharos: Disease Associations

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	ARM repeat-like	8054090	3000116	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Leukotriene A4 hydrolase N-terminal domain	8054087	3000390	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Metalloproteases (zincins) catalytic domain	8054088	3001975	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	ERAP1 insert domain	8054089	3002272	SCOP2B (2022-06-29)
B [auth C]	SCOP2 Family	ERAP1 C-terminal domain-like	8047041	4005418	SCOP2 (2022-06-29)
B [auth C]	SCOP2 Family	ERAP1 N-terminal domain-like	8054086	4007628	SCOP2 (2022-06-29)
B [auth C]	SCOP2 Family	ERAP1 catalytic domain-like	8054085	4007629	SCOP2 (2022-06-29)
B [auth C]	SCOP2 Family	ERAP1 insert domain-like	8054084	4007630	SCOP2 (2022-06-29)
B [auth C]	SCOP2 Superfamily	ARM repeat-like	8054090	3000116	SCOP2 (2022-06-29)
B [auth C]	SCOP2 Superfamily	Leukotriene A4 hydrolase N-terminal domain	8054087	3000390	SCOP2 (2022-06-29)
B [auth C]	SCOP2 Superfamily	Metalloproteases (zincins) catalytic domain	8054088	3001975	SCOP2 (2022-06-29)
B [auth C]	SCOP2 Superfamily	ERAP1 insert domain	8054089	3002272	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	F_UNCLASSIFIED	e5ab0A3	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: F_UNCLASSIFIED	ECOD (1.6)
A	PF17900	e5ab0A1	A: beta sandwiches	X: Baculovirus p35 protein-related (From Topology)	H: Baculovirus p35 protein-related (From Topology)	T: Baculovirus p35 protein-related	F: PF17900	ECOD (1.6)
A	PF11838	e5ab0A4	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: PF11838	ECOD (1.6)
A	PF01433	e5ab0A2	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: PF01433	ECOD (1.6)
B [auth C]	F_UNCLASSIFIED	e5ab0C4	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: F_UNCLASSIFIED	ECOD (1.6)
B [auth C]	PF17900	e5ab0C3	A: beta sandwiches	X: Baculovirus p35 protein-related (From Topology)	H: Baculovirus p35 protein-related (From Topology)	T: Baculovirus p35 protein-related	F: PF17900	ECOD (1.6)
B [auth C]	PF11838	e5ab0C1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: PF11838	ECOD (1.6)
B [auth C]	PF01433	e5ab0C2	A: mixed a+b and a/b	X: Zincin-like	H: Metalloproteases (zincins) catalytic domain (From Topology)	T: Metalloproteases (zincins) catalytic domain	F: PF01433	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.1730	Mainly Beta	Sandwich	Immunoglobulin-like	tricorn interacting facor f3 domain	CATH (4.3.0)
A	1.10.390.10	Mainly Alpha	Orthogonal Bundle	Neutral Protease	domain 2	CATH (4.3.0)
A	2.60.40.1910	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)
A	1.25.50.20	Mainly Alpha	Alpha Horseshoe	Zincin-like fold		CATH (4.3.0)
B [auth C]	2.60.40.1730	Mainly Beta	Sandwich	Immunoglobulin-like	tricorn interacting facor f3 domain	CATH (4.3.0)
B [auth C]	1.10.390.10	Mainly Alpha	Orthogonal Bundle	Neutral Protease	domain 2	CATH (4.3.0)
B [auth C]	2.60.40.1910	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)
B [auth C]	1.25.50.20	Mainly Alpha	Alpha Horseshoe	Zincin-like fold		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B [auth C]	PF11838	ERAP1-like C-terminal domain (ERAP1_C)	ERAP1-like C-terminal domain	This large domain is composed of 16 alpha helices organized as 8 HEAT-like repeats. This domain forms a concave face that faces towards the active site of the peptidase.	Domain
A, B [auth C]	PF01433	Peptidase family M1 domain (Peptidase_M1)	Peptidase family M1 domain	Members of this family are aminopeptidases. The members differ widely in specificity, hydrolysing acidic, basic or neutral N-terminal residues. This family includes leukotriene-A4 hydrolase Swiss:P09960, this enzyme also has an aminopeptidase activ ...	Members of this family are aminopeptidases. The members differ widely in specificity, hydrolysing acidic, basic or neutral N-terminal residues. This family includes leukotriene-A4 hydrolase Swiss:P09960, this enzyme also has an aminopeptidase activity [1].	Domain
A, B [auth C]	PF17900	Peptidase M1 N-terminal domain (Peptidase_M1_N)	Peptidase M1 N-terminal domain	This domain is found at the N-terminus of aminopeptidases from the M1 family.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B [auth C]	ENDOPLASMATIC RETICULUM AMINOPEPTIDASE 2	peptidase activity catalytic activity, acting on a protein metallopeptidase activity hydrolase activity catalytic activity endopeptidase activity binding peptide binding cation binding transition metal ion binding zinc ion binding ion binding metal ion binding small molecule binding peptidase activity catalytic activity, acting on a protein metallopeptidase activity hydrolase activity catalytic activity endopeptidase activity binding peptide binding cation binding transition metal ion binding zinc ion binding ion binding metal ion binding small molecule binding aminopeptidase activity metalloaminopeptidase activity exopeptidase activity metalloexopeptidase activity	cellular catabolic process organic substance metabolic process catabolic process cellular metabolic process metabolic process cellular process organic substance catabolic process peptide metabolic process peptide catabolic process multicellular organismal process system process circulatory system process regulation of blood pressure biological regulation cellular catabolic process organic substance metabolic process catabolic process cellular metabolic process metabolic process cellular process organic substance catabolic process peptide metabolic process peptide catabolic process multicellular organismal process system process circulatory system process regulation of blood pressure biological regulation regulation of biological quality blood circulation response to stimulus immune response immune system process adaptive immune response antigen processing and presentation antigen processing and presentation of endogenous peptide antigen antigen processing and presentation of peptide antigen via MHC class I antigen processing and presentation of peptide antigen antigen processing and presentation of endogenous antigen antigen processing and presentation of endogenous peptide antigen via MHC class I organonitrogen compound metabolic process proteolysis primary metabolic process protein metabolic process macromolecule metabolic process	membrane-bounded organelle intracellular anatomical structure membrane-enclosed lumen cellular anatomical entity intracellular membrane-bounded organelle endomembrane system intracellular organelle lumen endoplasmic reticulum lumen intracellular organelle organelle lumen organelle endoplasmic reticulum cytoplasm organelle subcompartment membrane-bounded organelle intracellular anatomical structure membrane-enclosed lumen cellular anatomical entity intracellular membrane-bounded organelle endomembrane system intracellular organelle lumen endoplasmic reticulum lumen intracellular organelle organelle lumen organelle endoplasmic reticulum cytoplasm organelle subcompartment membrane endoplasmic reticulum subcompartment nuclear outer membrane-endoplasmic reticulum membrane network organelle membrane endoplasmic reticulum membrane
C [auth E], D [auth F]	DG025	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B [auth C]	IPR001930	Peptidase M1, alanine aminopeptidase/leukotriene A4 hydrolase	Family
A, B [auth C]	IPR027268	Peptidase M4/M1, CTD superfamily	Homologous Superfamily
A, B [auth C]	IPR034016	Aminopeptidase N-type	Family
A, B [auth C]	IPR014782	Peptidase M1, membrane alanine aminopeptidase	Domain
A, B [auth C]	IPR045357	Aminopeptidase N-like , N-terminal domain	Domain
A, B [auth C]	IPR042097	Aminopeptidase N-like , N-terminal domain superfamliy	Homologous Superfamily
A, B [auth C]	IPR024571	ERAP1-like C-terminal domain	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B [auth C]	Pharos: Q6P179	Crohn disease ankylosing spondylitis psoriasis ileocolitis juvenile dermatomyositis lung carcinoma malignant mesothelioma acute myeloid leukemia osteosarcoma astrocytic tumor primitive neuroectodermal tumor Behcet disease Sjogren syndrome Crohn's disease of the ileum gastric cancer Crohn disease ankylosing spondylitis psoriasis ileocolitis juvenile dermatomyositis lung carcinoma malignant mesothelioma acute myeloid leukemia osteosarcoma astrocytic tumor primitive neuroectodermal tumor Behcet disease Sjogren syndrome Crohn's disease of the ileum gastric cancer head and neck cancer inflammatory bowel disease juvenile idiopathic arthritis malignant ependymoma medulloblastoma ovarian cancer attention deficit hyperactivity disorder, inattentive type tuberculosis chronic obstructive pulmonary disease Crohn's colitis cutaneous lupus erythematosus gastric carcinoma hypertensive disorder interstitial lung disease lung cancer malignant glioma oligodendroglioma anterior uveitis pilocytic astrocytoma atypical teratoid rhabdoid tumor common variable immunodeficiency esophageal adenocarcinoma glioblastoma

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 R01GM133198.