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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2J0T

Crystal Structure of the Catalytic Domain of MMP-1 in Complex with the Inhibitory Domain of TIMP-1

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
D	0008191	molecular_function	metalloendopeptidase inhibitor activity
E	0008191	molecular_function	metalloendopeptidase inhibitor activity
F	0008191	molecular_function	metalloendopeptidase inhibitor activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A1266

Chain	Residue
A	HIS168
A	ASP170
A	HIS183
A	HIS196

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A1267

Chain	Residue
A	HIS218
A	HIS222
A	HIS228
D	CYS1

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A1268

Chain	Residue
A	GLY190
A	GLY192
A	ASP194
A	ASP158

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A1269

Chain	Residue
A	ASP175
A	GLY176
A	GLY178
A	ASN180
A	ASP198
A	GLU201

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA A1270

Chain	Residue
A	ASP124
A	GLU199
A	GLU201

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B1267

Chain	Residue
B	HIS168
B	ASP170
B	HIS183
B	HIS196

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B1268

Chain	Residue
B	HIS218
B	HIS222
B	HIS228
E	CYS1

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA B1269

Chain	Residue
B	ASP158
B	GLY190
B	GLY192
B	ASP194

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B1270

Chain	Residue
B	ASP175
B	GLY176
B	GLY178
B	ASN180
B	ASP198
B	GLU201

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA B1271

Chain	Residue
B	ASP124
B	GLU199
B	GLU201

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C1264

Chain	Residue
C	HIS168
C	ASP170
C	HIS183
C	HIS196

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C1265

Chain	Residue
C	HIS218
C	HIS222
C	HIS228
F	CYS1

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA C1266

Chain	Residue
C	ASP158
C	GLY190
C	GLY192
C	ASP194

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C1267

Chain	Residue
C	ASP175
C	GLY176
C	GLY178
C	ASN180
C	ASP198
C	GLU201

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA C1268

Chain	Residue
C	ASP124
C	GLU199
C	GLU201

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL215-LEU224

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

Chain	Residue	Details
D	CYS1-CYS13

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:22427646

Chain	Residue	Details
D	CYS1
E	CYS1
F	CYS1

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

Chain	Residue	Details
D	LEU34
E	LEU34
F	LEU34

site_id	SWS_FT_FI3
Number of Residues	3
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
D	ASN30
E	ASN30
F	ASN30
B	ASP158
B	GLY190
B	ASP194
C	ASP158
C	GLY190
C	ASP194

site_id	SWS_FT_FI4
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16740002

Chain	Residue	Details
D	ASN78
B	HIS218
B	HIS222
B	HIS228
C	HIS168
C	HIS183
C	HIS196
C	HIS218
C	HIS222
C	HIS228
E	ASN78
F	ASN78
A	HIS218
A	HIS222
A	HIS228
B	HIS168
B	HIS183
B	HIS196

site_id	SWS_FT_FI5
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:15611040, ECO:0000269\|PubMed:7656013, ECO:0000269\|PubMed:8031754, ECO:0000269\|PubMed:8090713, ECO:0000269\|PubMed:8278810, ECO:0000269\|PubMed:9484219, ECO:0007744\|PDB:1CGE, ECO:0007744\|PDB:1CGF, ECO:0007744\|PDB:1CGL, ECO:0007744\|PDB:1HFC, ECO:0007744\|PDB:1SU3, ECO:0007744\|PDB:2AYK, ECO:0007744\|PDB:2CLT, ECO:0007744\|PDB:2J0T, ECO:0007744\|PDB:2TCL, ECO:0007744\|PDB:3SHI, ECO:0007744\|PDB:4AUO, ECO:0007744\|PDB:966C

Chain	Residue	Details
A	ASP170
B	ASP170
C	ASP170

site_id	SWS_FT_FI6
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:15611040, ECO:0000269\|PubMed:7656013, ECO:0000269\|PubMed:8031754, ECO:0000269\|PubMed:8090713, ECO:0000269\|PubMed:8278810, ECO:0007744\|PDB:1CGE, ECO:0007744\|PDB:1CGF, ECO:0007744\|PDB:1CGL, ECO:0007744\|PDB:1HFC, ECO:0007744\|PDB:1SU3, ECO:0007744\|PDB:2CLT, ECO:0007744\|PDB:2J0T, ECO:0007744\|PDB:2TCL, ECO:0007744\|PDB:3SHI, ECO:0007744\|PDB:4AUO, ECO:0007744\|PDB:966C

Chain	Residue	Details
A	ASP175
B	ASP175
C	ASP175

site_id	SWS_FT_FI7
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:15611040, ECO:0000269\|PubMed:7656013, ECO:0000269\|PubMed:8031754, ECO:0000269\|PubMed:8090713, ECO:0000269\|PubMed:8278810, ECO:0000269\|PubMed:9484219, ECO:0007744\|PDB:1AYK, ECO:0007744\|PDB:1CGE, ECO:0007744\|PDB:1CGF, ECO:0007744\|PDB:1CGL, ECO:0007744\|PDB:1HFC, ECO:0007744\|PDB:1SU3, ECO:0007744\|PDB:2AYK, ECO:0007744\|PDB:2CLT, ECO:0007744\|PDB:2J0T, ECO:0007744\|PDB:2TCL, ECO:0007744\|PDB:3SHI, ECO:0007744\|PDB:4AUO, ECO:0007744\|PDB:4AYK, ECO:0007744\|PDB:966C

Chain	Residue	Details
A	GLY176
B	GLY176
C	GLY176

site_id	SWS_FT_FI8
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:15611040, ECO:0000269\|PubMed:7656013, ECO:0000269\|PubMed:8031754, ECO:0000269\|PubMed:8090713, ECO:0000269\|PubMed:8278810, ECO:0000269\|PubMed:9484219, ECO:0007744\|PDB:1AYK, ECO:0007744\|PDB:1CGE, ECO:0007744\|PDB:1CGF, ECO:0007744\|PDB:1CGL, ECO:0007744\|PDB:1HFC, ECO:0007744\|PDB:1SU3, ECO:0007744\|PDB:2AYK, ECO:0007744\|PDB:2CLT, ECO:0007744\|PDB:2J0T, ECO:0007744\|PDB:2TCL, ECO:0007744\|PDB:3SHI, ECO:0007744\|PDB:4AUO, ECO:0007744\|PDB:966C

Chain	Residue	Details
A	GLY178
A	ASN180
B	GLY178
B	ASN180
C	GLY178
C	ASN180

site_id	SWS_FT_FI9
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:7656013, ECO:0000269\|PubMed:8031754, ECO:0007744\|PDB:1CGE, ECO:0007744\|PDB:1CGF, ECO:0007744\|PDB:2CLT, ECO:0007744\|PDB:2J0T, ECO:0007744\|PDB:2TCL, ECO:0007744\|PDB:4AUO, ECO:0007744\|PDB:966C

Chain	Residue	Details
A	GLY192
B	GLY192
C	GLY192

site_id	SWS_FT_FI10
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:15611040, ECO:0000269\|PubMed:7656013, ECO:0000269\|PubMed:8031754, ECO:0000269\|PubMed:8090713, ECO:0000269\|PubMed:8278810, ECO:0007744\|PDB:1CGE, ECO:0007744\|PDB:1CGF, ECO:0007744\|PDB:1CGL, ECO:0007744\|PDB:1HFC, ECO:0007744\|PDB:1SU3, ECO:0007744\|PDB:2CLT, ECO:0007744\|PDB:2J0T, ECO:0007744\|PDB:2TCL, ECO:0007744\|PDB:3AYK, ECO:0007744\|PDB:3SHI, ECO:0007744\|PDB:4AUO, ECO:0007744\|PDB:4AYK, ECO:0007744\|PDB:966C

Chain	Residue	Details
A	ASP198
B	ASP198
C	ASP198

site_id	SWS_FT_FI11
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:15611040, ECO:0000269\|PubMed:8031754, ECO:0007744\|PDB:1CGE, ECO:0007744\|PDB:1CGF, ECO:0007744\|PDB:1SU3, ECO:0007744\|PDB:2CLT, ECO:0007744\|PDB:2J0T, ECO:0007744\|PDB:3SHI, ECO:0007744\|PDB:4AUO, ECO:0007744\|PDB:966C

Chain	Residue	Details
A	GLU199
B	GLU199
C	GLU199

site_id	SWS_FT_FI12
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:15611040, ECO:0000269\|PubMed:7656013, ECO:0000269\|PubMed:8031754, ECO:0000269\|PubMed:8090713, ECO:0000269\|PubMed:8278810, ECO:0000269\|PubMed:9484219, ECO:0007744\|PDB:1AYK, ECO:0007744\|PDB:1CGE, ECO:0007744\|PDB:1CGF, ECO:0007744\|PDB:1CGL, ECO:0007744\|PDB:1HFC, ECO:0007744\|PDB:1SU3, ECO:0007744\|PDB:2AYK, ECO:0007744\|PDB:2CLT, ECO:0007744\|PDB:2J0T, ECO:0007744\|PDB:2TCL, ECO:0007744\|PDB:3AYK, ECO:0007744\|PDB:3SHI, ECO:0007744\|PDB:4AUO, ECO:0007744\|PDB:966C

Chain	Residue	Details
A	GLU201
B	GLU201
C	GLU201

site_id	SWS_FT_FI13
Number of Residues	3
Details	SITE: Not glycosylated => ECO:0000269\|PubMed:10092871

Chain	Residue	Details
A	ASN143
B	ASN143
C	ASN143

site_id	SWS_FT_FI14
Number of Residues	3
Details	SITE: Cleavage; by autolysis => ECO:0000269\|PubMed:2557822

Chain	Residue	Details
A	PRO269
B	PRO269
C	PRO269

site_id	SWS_FT_FI15
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:10092871

Chain	Residue	Details
A	ASN120
B	ASN120
C	ASN120

Catalytic Information from CSA

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

Chain	Residue	Details
A	MET236
A	GLU219

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
B	MET236
B	GLU219

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
C	MET236
C	GLU219

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
A	GLU219

site_id	CSA5
Number of Residues	1
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
B	GLU219

site_id	CSA6
Number of Residues	1
Details	Annotated By Reference To The Literature 1hfs

Chain	Residue	Details
C	GLU219

222415

PDB entries from 2024-07-10

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