5H0U
Crystal structure of the catalytic domain of membrane type 1 matrix metalloproteinase
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 301 |
| Chain | Residue |
| A | ASP176 |
| A | ASN208 |
| A | GLY210 |
| A | ASP212 |
| A | HOH429 |
| A | HOH433 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 302 |
| Chain | Residue |
| A | HOH411 |
| B | HIS33 |
| A | HIS239 |
| A | HIS243 |
| A | HIS249 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 303 |
| Chain | Residue |
| A | HIS186 |
| A | ASP188 |
| A | HIS201 |
| A | HIS214 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 304 |
| Chain | Residue |
| A | ASP193 |
| A | GLY194 |
| A | GLY196 |
| A | PHE198 |
| A | ASP216 |
| A | GLU219 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue EPE A 305 |
| Chain | Residue |
| A | PHE180 |
| A | HIS186 |
| A | SER254 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 306 |
| Chain | Residue |
| A | GLY136 |
| A | GLU137 |
| A | TYR138 |
| A | HOH432 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 307 |
| Chain | Residue |
| A | ARG145 |
| A | ARG149 |
| A | GLU152 |
| A | PHE159 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 308 |
| Chain | Residue |
| A | ASN208 |
| A | ASP212 |
| A | GLN262 |
| A | TRP263 |
| A | HOH415 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 309 |
| Chain | Residue |
| A | ALA165 |
| A | GLY246 |
| A | LEU247 |
| A | GLU248 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 310 |
| Chain | Residue |
| A | GLU183 |
| A | GLY184 |
| A | PHE192 |
| A | GLY194 |
| A | HOH426 |
| site_id | AD2 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 311 |
| Chain | Residue |
| A | LEU235 |
| A | VAL236 |
| A | HIS239 |
| A | GLU240 |
| A | PHE260 |
| A | TYR261 |
| A | GOL312 |
| A | HOH411 |
| A | HOH428 |
| B | HIS33 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 312 |
| Chain | Residue |
| A | GLY197 |
| A | PHE198 |
| A | LEU199 |
| A | PHE260 |
| A | TYR261 |
| A | GOL311 |
| A | GOL313 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 313 |
| Chain | Residue |
| A | GLY170 |
| A | GLU172 |
| A | LYS173 |
| A | ASP193 |
| A | GLY197 |
| A | PHE198 |
| A | GOL312 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 314 |
| Chain | Residue |
| A | HIS171 |
| A | GLU248 |
| B | HIS28 |
| B | HIS32 |
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 |
| A | VAL236-LEU245 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| 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 | 16 |
| 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 |
