7XGJ

Crystal structure of human MMP-2 catalytic domain in complex with inhibitor

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
A	0031012	cellular_component	extracellular matrix
B	0004222	molecular_function	metalloendopeptidase activity
B	0006508	biological_process	proteolysis
B	0008237	molecular_function	metallopeptidase activity
B	0008270	molecular_function	zinc ion binding
B	0031012	cellular_component	extracellular matrix
C	0004222	molecular_function	metalloendopeptidase activity
C	0006508	biological_process	proteolysis
C	0008237	molecular_function	metallopeptidase activity
C	0008270	molecular_function	zinc ion binding
C	0031012	cellular_component	extracellular matrix

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10356396","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21813640","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QIB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AYU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21813640","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EAK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AYU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10356396","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12032297","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21813640","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CK7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EAK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GXD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QIB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AYU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21813640","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3AYU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10356396","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12032297","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21813640","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CK7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EAK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GXD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AYU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 906

Chain	Residue	Details
A	HIS121	metal ligand
A	ALA122	proton shuttle (general acid/base)
A	HIS125	metal ligand
A	HIS131	metal ligand

---

site_id	MCSA2
Number of Residues	4
Details	M-CSA 906

Chain	Residue	Details
B	HIS121	metal ligand
B	ALA122	proton shuttle (general acid/base)
B	HIS125	metal ligand
B	HIS131	metal ligand

---

site_id	MCSA3
Number of Residues	4
Details	M-CSA 906

Chain	Residue	Details
C	HIS121	metal ligand
C	ALA122	proton shuttle (general acid/base)
C	HIS125	metal ligand
C	HIS131	metal ligand

---