1SU3
X-ray structure of human proMMP-1: New insights into collagenase action
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004175 | molecular_function | endopeptidase activity |
| A | 0004222 | molecular_function | metalloendopeptidase activity |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0022617 | biological_process | extracellular matrix disassembly |
| A | 0030198 | biological_process | extracellular matrix organization |
| A | 0030574 | biological_process | collagen catabolic process |
| A | 0031012 | cellular_component | extracellular matrix |
| A | 0031334 | biological_process | positive regulation of protein-containing complex assembly |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071492 | biological_process | cellular response to UV-A |
| B | 0004175 | molecular_function | endopeptidase activity |
| B | 0004222 | molecular_function | metalloendopeptidase activity |
| B | 0004252 | molecular_function | serine-type endopeptidase activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0006508 | biological_process | proteolysis |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0008237 | molecular_function | metallopeptidase activity |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0022617 | biological_process | extracellular matrix disassembly |
| B | 0030198 | biological_process | extracellular matrix organization |
| B | 0030574 | biological_process | collagen catabolic process |
| B | 0031012 | cellular_component | extracellular matrix |
| B | 0031334 | biological_process | positive regulation of protein-containing complex assembly |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071492 | biological_process | cellular response to UV-A |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 901 |
| Chain | Residue |
| A | ALA157 |
| A | ASP158 |
| A | GLY190 |
| A | GLY192 |
| A | ASP194 |
| A | HOH1027 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 902 |
| Chain | Residue |
| A | HOH946 |
| A | HOH991 |
| A | ASP124 |
| A | GLU199 |
| A | GLU201 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 903 |
| Chain | Residue |
| A | ASP175 |
| A | GLY176 |
| A | GLY178 |
| A | ASN180 |
| A | ASP198 |
| A | GLU201 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 904 |
| Chain | Residue |
| A | ASP285 |
| A | GLU329 |
| A | ASP378 |
| A | ASP427 |
| A | HOH916 |
| A | HOH961 |
| A | HOH1052 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 905 |
| Chain | Residue |
| B | ALA157 |
| B | ASP158 |
| B | GLY190 |
| B | GLY192 |
| B | ASP194 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 906 |
| Chain | Residue |
| B | ASP175 |
| B | GLY176 |
| B | GLY178 |
| B | ASN180 |
| B | ASP198 |
| B | GLU201 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 907 |
| Chain | Residue |
| B | ASP124 |
| B | GLU199 |
| B | GLU201 |
| B | HOH1085 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 908 |
| Chain | Residue |
| B | ASP285 |
| B | GLU329 |
| B | ASP378 |
| B | ASP427 |
| B | HOH1052 |
| B | HOH1053 |
| B | HOH1080 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 909 |
| Chain | Residue |
| A | ILE287 |
| A | ALA331 |
| A | ALA380 |
| A | VAL429 |
| A | NA911 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL B 910 |
| Chain | Residue |
| B | ILE287 |
| B | ALA331 |
| B | ALA380 |
| B | ALA428 |
| B | VAL429 |
| B | NA912 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 911 |
| Chain | Residue |
| A | ILE287 |
| A | ALA331 |
| A | ALA380 |
| A | VAL429 |
| A | CL909 |
| A | HOH1088 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 912 |
| Chain | Residue |
| B | ILE287 |
| B | ALA331 |
| B | ALA380 |
| B | VAL429 |
| B | CL910 |
| B | HOH980 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 913 |
| Chain | Residue |
| A | CYS92 |
| A | HIS218 |
| A | HIS222 |
| A | HIS228 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 915 |
| Chain | Residue |
| A | HIS168 |
| A | ASP170 |
| A | HIS183 |
| A | HIS196 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 913 |
| Chain | Residue |
| B | CYS92 |
| B | HIS218 |
| B | HIS222 |
| B | HIS228 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 915 |
| Chain | Residue |
| B | HIS168 |
| B | ASP170 |
| B | HIS183 |
| B | HIS196 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 500 |
| Chain | Residue |
| B | PRO189 |
| B | GLY190 |
| B | LYS404 |
| site_id | BC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 501 |
| Chain | Residue |
| B | ASP167 |
| B | HIS168 |
| B | ARG169 |
| B | ASP170 |
| B | ASN171 |
| B | PRO173 |
| B | HOH946 |
| site_id | CC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 504 |
| Chain | Residue |
| B | PRO126 |
| B | ARG127 |
| site_id | CC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 503 |
| Chain | Residue |
| B | SER263 |
| B | GLN264 |
| B | ASN265 |
| B | HOH918 |
| B | SER142 |
| B | THR145 |
| site_id | CC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 801 |
| Chain | Residue |
| A | PRO126 |
| A | ARG127 |
| A | LYS404 |
| A | HOH1050 |
| A | HOH1104 |
| site_id | CC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EPE B 600 |
| Chain | Residue |
| B | VAL94 |
| B | PRO95 |
| B | SER172 |
| B | ALA184 |
| B | PHE185 |
| B | GLN186 |
| B | HOH959 |
Functional Information from PROSITE/UniProt
| site_id | PS00024 |
| Number of Residues | 16 |
| Details | HEMOPEXIN Hemopexin domain signature. ISvfWpqlPnGLEAAY |
| Chain | Residue | Details |
| A | ILE317-TYR332 |
| 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 | PS00546 |
| Number of Residues | 8 |
| Details | CYSTEINE_SWITCH Matrixins cysteine switch. PRCGvPDV |
| Chain | Residue | Details |
| A | PRO90-VAL97 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: |
| Chain | Residue | Details |
| A | GLU219 | |
| B | GLU219 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: in inhibited form => ECO:0000269|PubMed:15611040, ECO:0007744|PDB:1SU3 |
| Chain | Residue | Details |
| A | CYS92 | |
| B | CYS92 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => 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:966C |
| Chain | Residue | Details |
| A | ASP124 | |
| B | ASP124 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15611040, ECO:0000269|PubMed:7656013, 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:2TCL, ECO:0007744|PDB:4AUO, ECO:0007744|PDB:966C |
| Chain | Residue | Details |
| A | ASP158 | |
| A | GLY190 | |
| A | ASP194 | |
| B | ASP158 | |
| B | GLY190 | |
| B | ASP194 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| 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:4AYK, ECO:0007744|PDB:966C |
| Chain | Residue | Details |
| A | HIS168 | |
| B | HIS218 | |
| B | HIS222 | |
| B | HIS228 | |
| A | HIS183 | |
| A | HIS196 | |
| A | HIS218 | |
| A | HIS222 | |
| A | HIS228 | |
| B | HIS168 | |
| B | HIS183 | |
| B | HIS196 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| 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 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| 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 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| 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 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| 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 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| 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 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| 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 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| 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 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| 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 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15611040, ECO:0007744|PDB:1SU3, ECO:0007744|PDB:2CLT, ECO:0007744|PDB:4AUO |
| Chain | Residue | Details |
| A | ASP285 | |
| A | GLU329 | |
| A | ASP378 | |
| A | ASP427 | |
| B | ASP285 | |
| B | GLU329 | |
| B | ASP378 | |
| B | ASP427 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | SITE: Not glycosylated => ECO:0000269|PubMed:10092871 |
| Chain | Residue | Details |
| A | ASN143 | |
| B | ASN143 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | SITE: Cleavage; by autolysis => ECO:0000269|PubMed:2557822 |
| Chain | Residue | Details |
| A | PRO269 | |
| B | PRO269 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:25171405 |
| Chain | Residue | Details |
| A | SER57 | |
| B | SER57 |
| site_id | SWS_FT_FI18 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:25171405 |
| Chain | Residue | Details |
| A | THR274 | |
| B | THR274 |
| site_id | SWS_FT_FI19 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine; by PKDCC => ECO:0000269|PubMed:25171405 |
| Chain | Residue | Details |
| A | TYR360 | |
| B | TYR360 |
| site_id | SWS_FT_FI20 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10092871 |
| Chain | Residue | Details |
| A | ASN120 | |
| B | 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 | 1 |
| Details | Annotated By Reference To The Literature 1hfs |
| Chain | Residue | Details |
| A | GLU219 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1hfs |
| Chain | Residue | Details |
| B | GLU219 |
