4JBS

Crystal structure of the human Endoplasmic Reticulum Aminopeptidase 2 in complex with PHOSPHINIC PSEUDOTRIPEPTIDE inhibitor.

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0005515	molecular_function	protein binding
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	0006508	biological_process	proteolysis
A	0008217	biological_process	regulation of blood pressure
A	0008237	molecular_function	metallopeptidase activity
A	0008270	molecular_function	zinc ion binding
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	0046872	molecular_function	metal ion binding
A	0070006	molecular_function	metalloaminopeptidase activity
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	0005515	molecular_function	protein binding
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	0006508	biological_process	proteolysis
B	0008217	biological_process	regulation of blood pressure
B	0008237	molecular_function	metallopeptidase activity
B	0008270	molecular_function	zinc ion binding
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	0046872	molecular_function	metal ion binding
B	0070006	molecular_function	metalloaminopeptidase activity

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL367-TRP376

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	38
Details	TRANSMEM: Helical; Signal-anchor for type II membrane protein => ECO:0000255

Chain	Residue	Details
A	GLY21-VAL40
B	GLY21-VAL40

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site_id	SWS_FT_FI2
Number of Residues	1838
Details	TOPO_DOM: Lumenal => ECO:0000255

Chain	Residue	Details
A	PRO41-THR960
B	PRO41-THR960

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site_id	SWS_FT_FI3
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:22106953

Chain	Residue	Details
A	GLU371
B	GLU371

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site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:22106953

Chain	Residue	Details
A	GLU200
B	GLU200

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site_id	SWS_FT_FI5
Number of Residues	8
Details	BINDING:

Chain	Residue	Details
A	HIS374
A	GLU393
B	GLY334
B	HIS370
B	HIS374
B	GLU393
A	GLY334
A	HIS370

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site_id	SWS_FT_FI6
Number of Residues	2
Details	SITE: Transition state stabilizer

Chain	Residue	Details
A	TYR455
B	TYR455

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site_id	SWS_FT_FI7
Number of Residues	8
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22106953

Chain	Residue	Details
A	ASN85
A	ASN219
A	ASN405
A	ASN650
B	ASN85
B	ASN219
B	ASN405
B	ASN650

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site_id	SWS_FT_FI8
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952

Chain	Residue	Details
A	ASN119
B	ASN119

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