830C
COLLAGENASE-3 (MMP-13) COMPLEXED TO A SULPHONE-BASED HYDROXAMIC ACID
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 272 |
| Chain | Residue |
| A | RS11 |
| A | HIS222 |
| A | HIS226 |
| A | HIS232 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 273 |
| Chain | Residue |
| A | HIS172 |
| A | ASP174 |
| A | HIS187 |
| A | HIS200 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 274 |
| Chain | Residue |
| A | GLY180 |
| A | SER182 |
| A | LEU184 |
| A | ASP202 |
| A | GLU205 |
| A | ASP179 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 272 |
| Chain | Residue |
| B | RS11 |
| B | HIS222 |
| B | HIS226 |
| B | HIS232 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 273 |
| Chain | Residue |
| B | HIS172 |
| B | ASP174 |
| B | HIS187 |
| B | HIS200 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 274 |
| Chain | Residue |
| B | ASP179 |
| B | GLY180 |
| B | SER182 |
| B | LEU184 |
| B | ASP202 |
| B | GLU205 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE RS1 A 1 |
| Chain | Residue |
| A | LEU185 |
| A | ALA186 |
| A | HIS222 |
| A | GLU223 |
| A | HIS226 |
| A | HIS232 |
| A | LEU239 |
| A | PHE241 |
| A | PRO242 |
| A | ILE243 |
| A | TYR244 |
| A | ZN272 |
| A | HOH443 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE RS1 B 1 |
| Chain | Residue |
| B | LEU185 |
| B | ALA186 |
| B | HIS222 |
| B | GLU223 |
| B | HIS226 |
| B | HIS232 |
| B | LEU239 |
| B | PHE241 |
| B | PRO242 |
| B | ILE243 |
| B | ZN272 |
| B | HOH415 |
Functional Information from PROSITE/UniProt
| site_id | PS00142 |
| Number of Residues | 10 |
| Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHEFGHSL |
| Chain | Residue | Details |
| A | VAL219-LEU228 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 140 |
| Details | Region: {"description":"Interaction with TIMP2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"23913860","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10926524","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10986126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15734645","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15780611","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17196980","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17623656","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19422229","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20005097","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20726512","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22689580","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23810497","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23913860","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8969305","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10926524","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10986126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15734645","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15780611","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17196980","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17623656","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19422229","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20005097","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20726512","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22689580","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23810497","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23913860","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"8576151","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1hfs |
| Chain | Residue | Details |
| A | GLU223 | |
| A | MET240 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1hfs |
| Chain | Residue | Details |
| B | GLU223 | |
| B | MET240 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1hfs |
| Chain | Residue | Details |
| A | GLU223 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1hfs |
| Chain | Residue | Details |
| B | GLU223 |
