3G5C

Structural and biochemical studies on the ectodomain of human ADAM22

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	PS00022
Number of Residues	12
Details	EGF_1 EGF-like domain signature 1. CvCnrHwiGSdC

Chain	Residue	Details
A	CYS700-CYS711

---

site_id	PS00427
Number of Residues	20
Details	DISINTEGRIN_1 Disintegrins signature. CsdGlCCk.KCkFqpmgtvCR

Chain	Residue	Details
A	CYS485-ARG504

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	398
Details	Domain: {"description":"Peptidase M12B","evidences":[{"source":"PROSITE-ProRule","id":"PRU00276","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	174
Details	Domain: {"description":"Disintegrin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00068","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	74
Details	Domain: {"description":"EGF-like"}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	6
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19692335","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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