3MA2
Complex membrane type-1 matrix metalloproteinase (MT1-MMP) with tissue inhibitor of metalloproteinase-1 (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 | 0008191 | molecular_function | metalloendopeptidase inhibitor activity |
| C | 0008191 | molecular_function | metalloendopeptidase inhibitor 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 293 |
| Chain | Residue |
| D | HOH23 |
| D | HOH26 |
| D | ASP176 |
| D | ASN208 |
| D | GLY210 |
| D | ASP212 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 294 |
| Chain | Residue |
| D | HIS249 |
| C | CYS301 |
| D | HIS239 |
| D | HIS243 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 295 |
| Chain | Residue |
| D | HIS186 |
| D | ASP188 |
| D | HIS201 |
| D | HIS214 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 296 |
| Chain | Residue |
| D | ASP193 |
| D | GLY194 |
| D | GLY196 |
| D | PHE198 |
| D | ASP216 |
| D | GLU219 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 293 |
| Chain | Residue |
| A | HOH64 |
| A | ASP176 |
| A | ASN208 |
| A | GLY210 |
| A | ASP212 |
| A | HOH312 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 294 |
| Chain | Residue |
| A | HIS239 |
| A | HIS243 |
| A | HIS249 |
| B | CYS301 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 295 |
| Chain | Residue |
| A | HIS186 |
| A | ASP188 |
| A | HIS201 |
| A | HIS214 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 296 |
| Chain | Residue |
| A | ASP193 |
| A | GLY194 |
| A | GLY196 |
| A | PHE198 |
| A | ASP216 |
| A | GLU219 |
Functional Information from PROSITE/UniProt
| site_id | PS00142 |
| Number of Residues | 10 |
| Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAVHELGHAL |
| Chain | Residue | Details |
| D | VAL236-LEU245 |
| site_id | PS00288 |
| Number of Residues | 13 |
| Details | TIMP Tissue inhibitors of metalloproteinases signature. CtCaPvHPQtaFC |
| Chain | Residue | Details |
| B | CYS301-CYS313 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"35177851","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9724659","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9724659","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BQQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BUV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Region: {"description":"Involved in metalloproteinase-binding","evidences":[{"source":"PubMed","id":"22427646","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3V96","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22427646","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Site: {"description":"Involved in metalloproteinase-binding","evidences":[{"source":"PubMed","id":"22427646","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3V96","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","featureId":"CAR_000002","evidences":[{"source":"PubMed","id":"16263699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16740002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000003","evidences":[{"source":"PubMed","id":"16740002","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
