2RJP
Crystal structure of ADAMTS4 with inhibitor bound
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 |
| B | 0004222 | molecular_function | metalloendopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0008237 | molecular_function | metallopeptidase activity |
| C | 0004222 | molecular_function | metalloendopeptidase activity |
| C | 0006508 | biological_process | proteolysis |
| C | 0008237 | molecular_function | metallopeptidase activity |
| D | 0004222 | molecular_function | metalloendopeptidase activity |
| D | 0006508 | biological_process | proteolysis |
| D | 0008237 | molecular_function | metallopeptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1 |
| Chain | Residue |
| A | HIS361 |
| A | HIS365 |
| A | HIS371 |
| A | 886510 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 2 |
| Chain | Residue |
| A | ASP320 |
| A | LEU321 |
| A | CYS327 |
| A | THR329 |
| A | GLU349 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 3 |
| Chain | Residue |
| A | GLU221 |
| A | ASP304 |
| A | ASP311 |
| A | CYS423 |
| A | ASP426 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 4 |
| Chain | Residue |
| A | HOH57 |
| A | GLU221 |
| A | ASP304 |
| A | ASP426 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1 |
| Chain | Residue |
| B | HIS361 |
| B | HIS365 |
| B | HIS371 |
| B | 886510 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 2 |
| Chain | Residue |
| B | ASP320 |
| B | LEU321 |
| B | CYS327 |
| B | THR329 |
| B | GLU349 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 3 |
| Chain | Residue |
| B | GLU221 |
| B | ASP304 |
| B | ASP311 |
| B | CYS423 |
| B | ASP426 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA B 4 |
| Chain | Residue |
| B | GLU221 |
| B | ASP304 |
| B | ASP426 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 1 |
| Chain | Residue |
| C | HIS361 |
| C | HIS365 |
| C | HIS371 |
| C | 886510 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA C 2 |
| Chain | Residue |
| C | ASP320 |
| C | LEU321 |
| C | CYS327 |
| C | THR329 |
| C | GLU349 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA C 3 |
| Chain | Residue |
| C | GLU221 |
| C | ASP304 |
| C | ASP311 |
| C | CYS423 |
| C | ASP426 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA C 4 |
| Chain | Residue |
| C | HOH33 |
| C | GLU221 |
| C | ASP304 |
| C | ASP426 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 1 |
| Chain | Residue |
| D | HIS361 |
| D | HIS365 |
| D | HIS371 |
| D | 886510 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA D 2 |
| Chain | Residue |
| D | ASP320 |
| D | LEU321 |
| D | CYS327 |
| D | THR329 |
| D | GLU349 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA D 3 |
| Chain | Residue |
| D | GLU221 |
| D | ASP304 |
| D | ASP311 |
| D | CYS423 |
| D | ASP426 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA D 4 |
| Chain | Residue |
| D | GLU221 |
| D | ASP304 |
| D | ASP426 |
| site_id | BC8 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE 886 B 510 |
| Chain | Residue |
| B | ZN1 |
| B | ALA252 |
| B | THR329 |
| B | LEU330 |
| B | GLY331 |
| B | PHE357 |
| B | HIS361 |
| B | GLN362 |
| B | HIS365 |
| B | HIS371 |
| B | VAL390 |
| B | ALA392 |
| B | PRO393 |
| B | VAL394 |
| B | VAL398 |
| B | HOH527 |
| B | HOH532 |
| B | HOH536 |
| site_id | BC9 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE 886 D 510 |
| Chain | Residue |
| D | ALA392 |
| D | PRO393 |
| D | VAL394 |
| D | MET395 |
| D | VAL398 |
| D | ZN1 |
| D | THR329 |
| D | LEU330 |
| D | GLY331 |
| D | MET332 |
| D | PHE357 |
| D | HIS361 |
| D | GLN362 |
| D | HIS365 |
| D | HIS371 |
| D | VAL390 |
| site_id | CC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE 886 C 510 |
| Chain | Residue |
| C | ZN1 |
| C | ALA252 |
| C | THR329 |
| C | LEU330 |
| C | GLY331 |
| C | MET332 |
| C | PHE357 |
| C | HIS361 |
| C | GLN362 |
| C | HIS365 |
| C | HIS371 |
| C | VAL390 |
| C | ALA392 |
| C | PRO393 |
| C | MET395 |
| C | VAL398 |
| site_id | CC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE 886 A 510 |
| Chain | Residue |
| A | ZN1 |
| A | ALA252 |
| A | THR329 |
| A | LEU330 |
| A | GLY331 |
| A | MET332 |
| A | PHE357 |
| A | HIS361 |
| A | GLN362 |
| A | HIS365 |
| A | HIS371 |
| A | VAL390 |
| A | ALA392 |
| A | PRO393 |
| A | VAL394 |
| A | VAL398 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00276","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18042673","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18042673","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
