5AB0

Crystal structure of aminopeptidase ERAP2 with ligand

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002250	biological_process	adaptive immune response
A	0002376	biological_process	immune system process
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	0005737	cellular_component	cytoplasm
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	0008233	molecular_function	peptidase activity
A	0008237	molecular_function	metallopeptidase activity
A	0008270	molecular_function	zinc ion binding
A	0016787	molecular_function	hydrolase activity
A	0019885	biological_process	antigen processing and presentation of endogenous peptide antigen via MHC class I
A	0043171	biological_process	peptide catabolic process
A	0046872	molecular_function	metal ion binding
A	0070006	molecular_function	metalloaminopeptidase activity
C	0002250	biological_process	adaptive immune response
C	0002376	biological_process	immune system process
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	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005788	cellular_component	endoplasmic reticulum lumen
C	0005789	cellular_component	endoplasmic reticulum membrane
C	0006508	biological_process	proteolysis
C	0008217	biological_process	regulation of blood pressure
C	0008233	molecular_function	peptidase activity
C	0008237	molecular_function	metallopeptidase activity
C	0008270	molecular_function	zinc ion binding
C	0016787	molecular_function	hydrolase activity
C	0019885	biological_process	antigen processing and presentation of endogenous peptide antigen via MHC class I
C	0043171	biological_process	peptide catabolic process
C	0046872	molecular_function	metal ion binding
C	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	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22106953","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22106953","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	14
Details	Binding site: {}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	2
Details	Site: {"description":"Transition state stabilizer"}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	8
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"22106953","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---