7XGJ
Crystal structure of human MMP-2 catalytic domain in complex with 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 |
| 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 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000305|PubMed:10356396 |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1QIB, ECO:0007744|PDB:3AYU |
| Chain | Residue | Details |
| A | ASP26 | |
| A | ASP101 | |
| B | ASP26 | |
| B | ASP101 | |
| C | ASP26 | |
| C | ASP101 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:3AYU |
| Chain | Residue | Details |
| A | ASP60 | |
| A | GLY92 | |
| B | ASP60 | |
| B | GLY92 | |
| C | ASP60 | |
| C | GLY92 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:12032297, ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:1GXD, ECO:0007744|PDB:1QIB, ECO:0007744|PDB:3AYU |
| Chain | Residue | Details |
| A | HIS70 | |
| C | ASP72 | |
| C | HIS85 | |
| C | HIS98 | |
| A | ASP72 | |
| A | HIS85 | |
| A | HIS98 | |
| B | HIS70 | |
| B | ASP72 | |
| B | HIS85 | |
| B | HIS98 | |
| C | HIS70 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21813640, ECO:0007744|PDB:3AYU |
| Chain | Residue | Details |
| A | ASP77 | |
| B | ASP96 | |
| B | ASP100 | |
| B | GLU103 | |
| C | ASP77 | |
| C | GLY78 | |
| C | GLY94 | |
| C | ASP96 | |
| C | ASP100 | |
| C | GLU103 | |
| A | GLY78 | |
| A | GLY94 | |
| A | ASP96 | |
| A | ASP100 | |
| A | GLU103 | |
| B | ASP77 | |
| B | GLY78 | |
| B | GLY94 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 9 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:12032297, ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:1GXD, ECO:0007744|PDB:3AYU |
| Chain | Residue | Details |
