Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1UEA

MMP-3/TIMP-1 COMPLEX

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	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	0010466	biological_process	negative regulation of peptidase activity
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	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	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	2001044	biological_process	regulation of integrin-mediated signaling pathway
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
D	0002020	molecular_function	protease binding
D	0002248	biological_process	connective tissue replacement involved in inflammatory response wound healing
D	0005125	molecular_function	cytokine activity
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005604	cellular_component	basement membrane
D	0005615	cellular_component	extracellular space
D	0005788	cellular_component	endoplasmic reticulum lumen
D	0007165	biological_process	signal transduction
D	0008083	molecular_function	growth factor activity
D	0008191	molecular_function	metalloendopeptidase inhibitor activity
D	0008270	molecular_function	zinc ion binding
D	0008284	biological_process	positive regulation of cell population proliferation
D	0009725	biological_process	response to hormone
D	0010466	biological_process	negative regulation of peptidase activity
D	0010951	biological_process	negative regulation of endopeptidase activity
D	0030414	molecular_function	peptidase inhibitor activity
D	0031012	cellular_component	extracellular matrix
D	0031093	cellular_component	platelet alpha granule lumen
D	0034097	biological_process	response to cytokine
D	0043066	biological_process	negative regulation of apoptotic process
D	0043086	biological_process	negative regulation of catalytic activity
D	0043434	biological_process	response to peptide hormone
D	0046872	molecular_function	metal ion binding
D	0051045	biological_process	negative regulation of membrane protein ectodomain proteolysis
D	0051216	biological_process	cartilage development
D	0070062	cellular_component	extracellular exosome
D	0071492	biological_process	cellular response to UV-A
D	1901164	biological_process	negative regulation of trophoblast cell migration
D	1901653	biological_process	cellular response to peptide
D	1905049	biological_process	negative regulation of metallopeptidase activity
D	2001044	biological_process	regulation of integrin-mediated signaling pathway

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 1

Chain	Residue
A	HIS201
A	HIS205
A	HIS211
B	CYS1

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 2

Chain	Residue
A	HIS151
A	ASP153
A	HIS166
A	HIS179

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 3

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

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 4

Chain	Residue
A	ASP141
A	GLY173
A	ASN175
A	ASP177

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 5

Chain	Residue
A	ASP107
A	ASP182
A	ASP183
A	GLU184
A	HOH1337

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 1

Chain	Residue
C	HIS201
C	HIS205
C	HIS211
D	CYS1

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 2

Chain	Residue
C	HIS151
C	ASP153
C	HIS166
C	HIS179

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 3

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

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA C 4

Chain	Residue
C	ALA140
C	ASP141
C	GLY173
C	ASN175
C	ASP177

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA C 5

Chain	Residue
C	ASP107
C	ASP182
C	GLU184
C	GLN185

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	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:22427646

Chain	Residue	Details
B	CYS1
D	CYS1

site_id	SWS_FT_FI2
Number of Residues	4
Details	SITE: Involved in metalloproteinase-binding => ECO:0000269\|PubMed:22427646, ECO:0007744\|PDB:3V96

Chain	Residue	Details
B	LEU34
A	GLY173
A	ASN175
A	ASP177
A	HIS179
A	ASP181
A	ASP182
A	GLU184
C	ASP107
C	ASP141
C	HIS151
B	ILE135
C	ASP153
C	ASP158
C	GLY159
C	GLY161
C	VAL163
C	HIS166
C	GLY173
C	ASN175
C	ASP177
C	HIS179
D	LEU34
C	ASP181
C	ASP182
C	GLU184
D	ILE135
A	ASP158
A	GLY159
A	GLY161
A	VAL163
A	HIS166

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine; by FAM20C => ECO:0000269\|PubMed:26091039

Chain	Residue	Details
B	SER155
D	SER155
A	HIS211
C	HIS201
C	HIS205
C	HIS211

site_id	SWS_FT_FI4
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269\|PubMed:16263699, ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:16740002, ECO:0000269\|PubMed:19139490

Chain	Residue	Details
B	ALA30
D	ALA30

site_id	SWS_FT_FI5
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16740002

Chain	Residue	Details
B	ALA78
D	ALA78

Catalytic Information from CSA

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

Chain	Residue	Details
A	GLU202

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
C	GLU202

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

site_id	MCSA2
Number of Residues	4
Details	M-CSA 591

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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)