4ILW
Complex of matrix metalloproteinase-10 catalytic domain (MMP-10cd) with tissue inhibitor of metalloproteinases-2 (TIMP-2)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0002020 | molecular_function | protease binding |
| A | 0004857 | molecular_function | enzyme inhibitor activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0008191 | molecular_function | metalloendopeptidase inhibitor activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009725 | biological_process | response to hormone |
| A | 0030414 | molecular_function | peptidase inhibitor activity |
| A | 0031012 | cellular_component | extracellular matrix |
| A | 0034097 | biological_process | response to cytokine |
| A | 0034774 | cellular_component | secretory granule lumen |
| A | 0035580 | cellular_component | specific granule lumen |
| A | 0045861 | biological_process | negative regulation of proteolysis |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051045 | biological_process | negative regulation of membrane protein ectodomain proteolysis |
| A | 0140678 | molecular_function | molecular function inhibitor activity |
| A | 1904724 | cellular_component | tertiary granule lumen |
| A | 1904813 | cellular_component | ficolin-1-rich granule lumen |
| A | 1905049 | biological_process | negative regulation of metallopeptidase activity |
| B | 0002020 | molecular_function | protease binding |
| B | 0004857 | molecular_function | enzyme inhibitor activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0008191 | molecular_function | metalloendopeptidase inhibitor activity |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009725 | biological_process | response to hormone |
| B | 0030414 | molecular_function | peptidase inhibitor activity |
| B | 0031012 | cellular_component | extracellular matrix |
| B | 0034097 | biological_process | response to cytokine |
| B | 0034774 | cellular_component | secretory granule lumen |
| B | 0035580 | cellular_component | specific granule lumen |
| 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 | 0140678 | molecular_function | molecular function inhibitor activity |
| B | 1904724 | cellular_component | tertiary granule lumen |
| B | 1904813 | cellular_component | ficolin-1-rich granule lumen |
| B | 1905049 | biological_process | negative regulation of metallopeptidase activity |
| D | 0004222 | molecular_function | metalloendopeptidase activity |
| D | 0006508 | biological_process | proteolysis |
| D | 0008237 | molecular_function | metallopeptidase activity |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0031012 | cellular_component | extracellular matrix |
| F | 0004222 | molecular_function | metalloendopeptidase activity |
| F | 0006508 | biological_process | proteolysis |
| F | 0008237 | molecular_function | metallopeptidase activity |
| F | 0008270 | molecular_function | zinc ion binding |
| F | 0031012 | cellular_component | extracellular matrix |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 301 |
| Chain | Residue |
| A | CYS1 |
| D | HIS217 |
| D | HIS221 |
| D | HIS227 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 302 |
| Chain | Residue |
| D | HIS167 |
| D | ASP169 |
| D | HIS182 |
| D | HIS195 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 303 |
| Chain | Residue |
| D | GLY175 |
| D | GLY177 |
| D | SER179 |
| D | ASP197 |
| D | GLU200 |
| D | ASP174 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA D 304 |
| Chain | Residue |
| D | ASP157 |
| D | GLY189 |
| D | TYR191 |
| D | ASP193 |
| D | HOH410 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA D 305 |
| Chain | Residue |
| D | ASP123 |
| D | ASP198 |
| D | GLU200 |
| D | HOH425 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN F 301 |
| Chain | Residue |
| B | CYS1 |
| F | HIS217 |
| F | HIS221 |
| F | HIS227 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN F 302 |
| Chain | Residue |
| F | HIS167 |
| F | ASP169 |
| F | HIS182 |
| F | HIS195 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA F 303 |
| Chain | Residue |
| F | ASP174 |
| F | GLY175 |
| F | GLY177 |
| F | SER179 |
| F | ASP197 |
| F | GLU200 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA F 304 |
| Chain | Residue |
| F | ASP157 |
| F | GLY189 |
| F | TYR191 |
| F | ASP193 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA F 305 |
| Chain | Residue |
| F | ASP123 |
| F | ASP198 |
| F | GLU200 |
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 |
| D | VAL214-LEU223 |
| site_id | PS00288 |
| Number of Residues | 13 |
| Details | TIMP Tissue inhibitors of metalloproteinases signature. CsCsPvHPQqaFC |
| Chain | Residue | Details |
| A | CYS1-CYS13 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 250 |
| Details | Domain: {"description":"NTR","evidences":[{"source":"PROSITE-ProRule","id":"PRU00295","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Region: {"description":"Involved in metalloproteinase-binding","evidences":[{"source":"PubMed","id":"24073280","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ILW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24073280","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ILW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Site: {"description":"Involved in metalloproteinase-binding","evidences":[{"source":"PubMed","id":"24073280","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ILW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15095982","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 14 |
| Details | Binding site: {} |
| Chain | Residue | Details |






