Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3QNF

Crystal structure of the open state of human endoplasmic reticulum aminopeptidase 1 ERAP1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001525	biological_process	angiogenesis
A	0002250	biological_process	adaptive immune response
A	0002474	biological_process	antigen processing and presentation of peptide antigen via MHC class I
A	0004175	molecular_function	endopeptidase activity
A	0004177	molecular_function	aminopeptidase activity
A	0005138	molecular_function	interleukin-6 receptor binding
A	0005151	molecular_function	interleukin-1, type II receptor binding
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005737	cellular_component	cytoplasm
A	0005783	cellular_component	endoplasmic reticulum
A	0005788	cellular_component	endoplasmic reticulum lumen
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0005829	cellular_component	cytosol
A	0006508	biological_process	proteolysis
A	0006509	biological_process	membrane protein ectodomain proteolysis
A	0008217	biological_process	regulation of blood pressure
A	0008233	molecular_function	peptidase activity
A	0008235	molecular_function	metalloexopeptidase activity
A	0008237	molecular_function	metallopeptidase activity
A	0008270	molecular_function	zinc ion binding
A	0009617	biological_process	response to bacterium
A	0016020	cellular_component	membrane
A	0019885	biological_process	antigen processing and presentation of endogenous peptide antigen via MHC class I
A	0042277	molecular_function	peptide binding
A	0043171	biological_process	peptide catabolic process
A	0045088	biological_process	regulation of innate immune response
A	0045444	biological_process	fat cell differentiation
A	0045766	biological_process	positive regulation of angiogenesis
A	0046872	molecular_function	metal ion binding
A	0070006	molecular_function	metalloaminopeptidase activity
A	0070062	cellular_component	extracellular exosome
B	0001525	biological_process	angiogenesis
B	0002250	biological_process	adaptive immune response
B	0002474	biological_process	antigen processing and presentation of peptide antigen via MHC class I
B	0004175	molecular_function	endopeptidase activity
B	0004177	molecular_function	aminopeptidase activity
B	0005138	molecular_function	interleukin-6 receptor binding
B	0005151	molecular_function	interleukin-1, type II receptor binding
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005737	cellular_component	cytoplasm
B	0005783	cellular_component	endoplasmic reticulum
B	0005788	cellular_component	endoplasmic reticulum lumen
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0005829	cellular_component	cytosol
B	0006508	biological_process	proteolysis
B	0006509	biological_process	membrane protein ectodomain proteolysis
B	0008217	biological_process	regulation of blood pressure
B	0008233	molecular_function	peptidase activity
B	0008235	molecular_function	metalloexopeptidase activity
B	0008237	molecular_function	metallopeptidase activity
B	0008270	molecular_function	zinc ion binding
B	0009617	biological_process	response to bacterium
B	0016020	cellular_component	membrane
B	0019885	biological_process	antigen processing and presentation of endogenous peptide antigen via MHC class I
B	0042277	molecular_function	peptide binding
B	0043171	biological_process	peptide catabolic process
B	0045088	biological_process	regulation of innate immune response
B	0045444	biological_process	fat cell differentiation
B	0045766	biological_process	positive regulation of angiogenesis
B	0046872	molecular_function	metal ion binding
B	0070006	molecular_function	metalloaminopeptidase activity
B	0070062	cellular_component	extracellular exosome
C	0001525	biological_process	angiogenesis
C	0002250	biological_process	adaptive immune response
C	0002474	biological_process	antigen processing and presentation of peptide antigen via MHC class I
C	0004175	molecular_function	endopeptidase activity
C	0004177	molecular_function	aminopeptidase activity
C	0005138	molecular_function	interleukin-6 receptor binding
C	0005151	molecular_function	interleukin-1, type II receptor binding
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005615	cellular_component	extracellular space
C	0005737	cellular_component	cytoplasm
C	0005783	cellular_component	endoplasmic reticulum
C	0005788	cellular_component	endoplasmic reticulum lumen
C	0005789	cellular_component	endoplasmic reticulum membrane
C	0005829	cellular_component	cytosol
C	0006508	biological_process	proteolysis
C	0006509	biological_process	membrane protein ectodomain proteolysis
C	0008217	biological_process	regulation of blood pressure
C	0008233	molecular_function	peptidase activity
C	0008235	molecular_function	metalloexopeptidase activity
C	0008237	molecular_function	metallopeptidase activity
C	0008270	molecular_function	zinc ion binding
C	0009617	biological_process	response to bacterium
C	0016020	cellular_component	membrane
C	0019885	biological_process	antigen processing and presentation of endogenous peptide antigen via MHC class I
C	0042277	molecular_function	peptide binding
C	0043171	biological_process	peptide catabolic process
C	0045088	biological_process	regulation of innate immune response
C	0045444	biological_process	fat cell differentiation
C	0045766	biological_process	positive regulation of angiogenesis
C	0046872	molecular_function	metal ion binding
C	0070006	molecular_function	metalloaminopeptidase activity
C	0070062	cellular_component	extracellular exosome

Functional Information from PROSITE/UniProt

site_id	PS00142
Number of Residues	10
Details	ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TVAHELAHQW

Chain	Residue	Details
A	THR350-TRP359

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	TOPO_DOM: Cytoplasmic => ECO:0000255

Chain	Residue	Details
A	MET1
B	MET1
C	MET1

site_id	SWS_FT_FI2
Number of Residues	57
Details	TRANSMEM: Helical; Signal-anchor for type II membrane protein => ECO:0000255

Chain	Residue	Details
A	VAL2-LEU21
B	VAL2-LEU21
C	VAL2-LEU21

site_id	SWS_FT_FI3
Number of Residues	2757
Details	TOPO_DOM: Lumenal => ECO:0000255

Chain	Residue	Details
A	ALA22-MET941
B	ALA22-MET941
C	ALA22-MET941

site_id	SWS_FT_FI4
Number of Residues	3
Details	ACT_SITE: Proton acceptor => ECO:0000255\|PROSITE-ProRule:PRU10095

Chain	Residue	Details
A	GLU354
B	GLU354
C	GLU354

site_id	SWS_FT_FI5
Number of Residues	6
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	GLU183
A	GLY317
B	GLU183
B	GLY317
C	GLU183
C	GLY317

site_id	SWS_FT_FI6
Number of Residues	9
Details	BINDING:

Chain	Residue	Details
A	HIS353
A	HIS357
A	GLU376
B	HIS353
B	HIS357
B	GLU376
C	HIS353
C	HIS357
C	GLU376

site_id	SWS_FT_FI7
Number of Residues	3
Details	SITE: Transition state stabilizer => ECO:0000250

Chain	Residue	Details
A	TYR438
B	TYR438
C	TYR438

site_id	SWS_FT_FI8
Number of Residues	6
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:21478864, ECO:0000269\|Ref.16

Chain	Residue	Details
A	ASN70
A	ASN154
B	ASN70
B	ASN154
C	ASN70
C	ASN154

site_id	SWS_FT_FI9
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:19159218, ECO:0000269\|Ref.16

Chain	Residue	Details
A	ASN414
B	ASN414
C	ASN414

site_id	SWS_FT_FI10
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:21478864

Chain	Residue	Details
A	ASN760
B	ASN760
C	ASN760

site_id	SWS_FT_FI11
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN901
B	ASN901
C	ASN901

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)