3EDG

Crystal structure of bone morphogenetic protein 1 protease domain

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
A	0008270	molecular_function	zinc ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACE A 201

Chain	Residue
A	ALA1
A	ALA2
A	GLU103
A	ARG106
A	SER136
A	GLN189

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN A 210

Chain	Residue
A	HIS92
A	HIS96
A	HIS102

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 211

Chain	Residue
A	GLU103
A	GLN189
A	HOH214
A	HOH218
A	HOH221

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE89-VAL98

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01211","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18824173","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01211","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18824173","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ast

Chain	Residue	Details
A	TYR149
A	GLU93

---