2ERO

Crystal structure of vascular apoptosis-inducing protein-1(orthorhombic crystal form)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004222	molecular_function	metalloendopeptidase activity
A	0006508	biological_process	proteolysis
A	0008237	molecular_function	metallopeptidase activity
B	0004222	molecular_function	metalloendopeptidase activity
B	0006508	biological_process	proteolysis
B	0008237	molecular_function	metallopeptidase activity

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ALA332-LEU341

---

site_id	PS00427
Number of Residues	20
Details	DISINTEGRIN_1 Disintegrins signature. CaeGlCCd.QCrFkgagteCR

Chain	Residue	Details
A	CYS443-ARG462

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	392
Details	Domain: {"description":"Peptidase M12B","evidences":[{"source":"PROSITE-ProRule","id":"PRU00276","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	170
Details	Domain: {"description":"Disintegrin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00068","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	22
Details	Motif: {"description":"Metal-binding","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Motif: {"description":"D/ECD-tripeptide"}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00276","evidenceCode":"ECO:0000255"},{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00276","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16688218","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ERO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ERP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ERQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	22
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16688218","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ERO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ERP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ERQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Pyrrolidone carboxylic acid (Glu)","evidences":[{"source":"UniProtKB","id":"P0DM89","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16688218","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ERO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ERP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ERQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---