7S7M

Complex of tissue inhibitor of metalloproteinases-1 (TIMP-1) mutant (L34G/M66D/T98G/P131S/Q153N) with matrix metalloproteinase-3 catalytic domain (MMP-3cd)

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	0002020	molecular_function	protease binding
B	0002248	biological_process	connective tissue replacement involved in inflammatory response wound healing
B	0004857	molecular_function	enzyme inhibitor activity
B	0005125	molecular_function	cytokine activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005604	cellular_component	basement membrane
B	0005615	cellular_component	extracellular space
B	0005788	cellular_component	endoplasmic reticulum lumen
B	0007165	biological_process	signal transduction
B	0008083	molecular_function	growth factor activity
B	0008191	molecular_function	metalloendopeptidase inhibitor activity
B	0008270	molecular_function	zinc ion binding
B	0008284	biological_process	positive regulation of cell population proliferation
B	0009725	biological_process	response to hormone
B	0010951	biological_process	negative regulation of endopeptidase activity
B	0030414	molecular_function	peptidase inhibitor activity
B	0031012	cellular_component	extracellular matrix
B	0031093	cellular_component	platelet alpha granule lumen
B	0034097	biological_process	response to cytokine
B	0034774	cellular_component	secretory granule lumen
B	0043066	biological_process	negative regulation of apoptotic process
B	0043086	biological_process	negative regulation of catalytic activity
B	0043434	biological_process	response to peptide hormone
B	0045861	biological_process	negative regulation of proteolysis
B	0046872	molecular_function	metal ion binding
B	0051045	biological_process	negative regulation of membrane protein ectodomain proteolysis
B	0051216	biological_process	cartilage development
B	0070062	cellular_component	extracellular exosome
B	0071492	biological_process	cellular response to UV-A
B	1901164	biological_process	negative regulation of trophoblast cell migration
B	1901653	biological_process	cellular response to peptide
B	1905049	biological_process	negative regulation of metallopeptidase activity
B	1905641	biological_process	cellular response to acetaldehyde
B	2001044	biological_process	regulation of integrin-mediated signaling pathway

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue CA A 301

Chain	Residue
A	ASP141
A	GLY173
A	ASN175
A	ASP177
A	HOH401
A	HOH405

---

site_id	AC2
Number of Residues	4
Details	binding site for residue CA A 302

Chain	Residue
A	HOH410
A	ASP107
A	ASP182
A	GLU184

---

site_id	AC3
Number of Residues	6
Details	binding site for residue CA A 303

Chain	Residue
A	ASP158
A	GLY159
A	GLY161
A	VAL163
A	ASP181
A	GLU184

---

site_id	AC4
Number of Residues	4
Details	binding site for residue ZN A 304

Chain	Residue
A	HIS201
A	HIS205
A	HIS211
B	CYS1

---

site_id	AC5
Number of Residues	4
Details	binding site for residue ZN A 305

Chain	Residue
A	HIS151
A	ASP153
A	HIS166
A	HIS179

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL198-LEU207

---

site_id	PS00288
Number of Residues	13
Details	TIMP Tissue inhibitors of metalloproteinases signature. CtCvPpHPQtaFC

Chain	Residue	Details
B	CYS1-CYS13

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8740360","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	5
Details	Region: {"description":"Involved in metalloproteinase-binding","evidences":[{"source":"PubMed","id":"22427646","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3V96","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22427646","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Site: {"description":"Involved in metalloproteinase-binding","evidences":[{"source":"PubMed","id":"22427646","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3V96","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","featureId":"CAR_000002","evidences":[{"source":"PubMed","id":"16263699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16740002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000003","evidences":[{"source":"PubMed","id":"16740002","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 591

Chain	Residue	Details
A	HIS201	metal ligand
A	GLU202	proton acceptor, proton donor
A	HIS205	metal ligand
A	HIS211	metal ligand

---