2OW9
Crystal structure analysis of the MMP13 catalytic domain in complex with specific 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 601 |
| Chain | Residue |
| A | HIS201 |
| A | HIS205 |
| A | HIS211 |
| A | HAE502 |
| A | HOH836 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 602 |
| Chain | Residue |
| A | HIS151 |
| A | ASP153 |
| A | HIS166 |
| A | HIS179 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 603 |
| Chain | Residue |
| A | ASP158 |
| A | GLY159 |
| A | SER161 |
| A | LEU163 |
| A | ASP181 |
| A | GLU184 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 604 |
| Chain | Residue |
| A | ASP141 |
| A | ASN173 |
| A | GLY175 |
| A | ASP177 |
| A | HOH702 |
| A | HOH726 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA A 605 |
| Chain | Residue |
| A | ASP107 |
| A | ASP182 |
| A | GLU184 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 606 |
| Chain | Residue |
| B | HIS201 |
| B | HIS205 |
| B | HIS211 |
| B | HAE502 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 607 |
| Chain | Residue |
| B | HIS151 |
| B | ASP153 |
| B | HIS166 |
| B | HIS179 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 608 |
| Chain | Residue |
| B | ASP158 |
| B | GLY159 |
| B | SER161 |
| B | LEU163 |
| B | ASP181 |
| B | GLU184 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 609 |
| Chain | Residue |
| B | ASP141 |
| B | ASN173 |
| B | GLY175 |
| B | ASP177 |
| B | HOH621 |
| B | HOH630 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 610 |
| Chain | Residue |
| B | ASP107 |
| B | ASP182 |
| B | GLU184 |
| B | HOH629 |
| B | HOH653 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 611 |
| Chain | Residue |
| B | HIS110 |
| B | GLU114 |
| B | HIS230 |
| B | HOH789 |
| B | HOH790 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 701 |
| Chain | Residue |
| A | LYS118 |
| A | ARG134 |
| A | HOH713 |
| A | HOH722 |
| A | HOH802 |
| A | HOH808 |
| A | HOH893 |
| site_id | BC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE SP6 A 501 |
| Chain | Residue |
| A | LEU197 |
| A | HIS201 |
| A | ALA217 |
| A | LEU218 |
| A | PHE220 |
| A | ILE222 |
| A | TYR223 |
| A | THR224 |
| A | TYR225 |
| A | THR226 |
| A | LYS228 |
| A | SER229 |
| A | HIS230 |
| A | PHE231 |
| A | MET232 |
| A | HOH712 |
| site_id | BC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE SP6 B 501 |
| Chain | Residue |
| B | LEU197 |
| B | HIS201 |
| B | ALA217 |
| B | LEU218 |
| B | PHE220 |
| B | ILE222 |
| B | TYR223 |
| B | THR224 |
| B | TYR225 |
| B | THR226 |
| B | LYS228 |
| B | SER229 |
| B | HIS230 |
| B | PHE231 |
| B | MET232 |
| B | HAE502 |
| B | HOH635 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE HAE A 502 |
| Chain | Residue |
| A | ZN601 |
| A | HOH708 |
| A | HOH836 |
| A | ALA165 |
| A | HIS201 |
| A | GLU202 |
| A | HIS205 |
| A | HIS211 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE HAE B 502 |
| Chain | Residue |
| B | ALA165 |
| B | HIS201 |
| B | GLU202 |
| B | HIS211 |
| B | PRO221 |
| B | SP6501 |
| B | ZN606 |
| B | HOH663 |
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 | VAL198-LEU207 |
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 | MET219 | |
| A | GLU202 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1hfs |
| Chain | Residue | Details |
| B | MET219 | |
| B | GLU202 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1hfs |
| Chain | Residue | Details |
| A | GLU202 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1hfs |
| Chain | Residue | Details |
| B | GLU202 |
