3AYU

Crystal structure of MMP-2 active site mutant in complex with APP-drived decapeptide 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

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 415

Chain	Residue
A	HIS120
A	HIS124
A	HIS130
B	ASP6

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 416

Chain	Residue
A	HIS69
A	ASP71
A	HIS84
A	HIS97

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 417

Chain	Residue
A	GLY77
A	ASP79
A	LEU81
A	ASP99
A	GLU102
A	ASP76

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 418

Chain	Residue
A	ASP59
A	GLY91
A	GLY93
A	ASP95
A	HOH212
A	HOH303

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 419

Chain	Residue
A	ASP25
A	ASP100
A	GLU102
A	HOH215

---

site_id	AC6
Number of Residues	40
Details	BINDING SITE FOR CHAIN B OF AMYLOID BETA A4 PROTEIN

Chain	Residue
A	PHE4
A	ASP32
A	ARG52
A	HIS54
A	TYR73
A	ALA83
A	HIS84
A	ALA85
A	PHE86
A	ALA87
A	VAL92
A	GLY93
A	TYR112
A	HIS120
A	HIS124
A	HIS130
A	PRO140
A	ILE141
A	TYR142
A	ASN147
A	HOH208
A	HOH274
A	HOH280
A	HOH336
A	HOH345
A	HOH371
A	ZN415
B	HOH42
B	HOH46
B	HOH52
B	HOH79
B	HOH82
B	HOH104
B	HOH170
B	HOH178
B	HOH202
B	HOH226
B	HOH227
B	HOH264
B	HOH267

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
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	2
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	2
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	4
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	6
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	3
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

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 906

Chain	Residue	Details
A	HIS120	metal ligand
A	ALA121	proton shuttle (general acid/base)
A	HIS124	metal ligand
A	HIS130	metal ligand

---