3HY7
Crystal Structure of the Catalytic Domain of ADAMTS-5 in Complex with Marimastat
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 097 A 801 |
| Chain | Residue |
| A | ASP377 |
| A | SER441 |
| A | ILE442 |
| A | LEU443 |
| A | ZN901 |
| A | HOH5007 |
| A | HOH5051 |
| A | HOH5155 |
| A | HOH5184 |
| A | THR378 |
| A | LEU379 |
| A | GLY380 |
| A | HIS410 |
| A | GLU411 |
| A | HIS414 |
| A | HIS420 |
| A | SER440 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 901 |
| Chain | Residue |
| A | HIS410 |
| A | HIS414 |
| A | HIS420 |
| A | 097801 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 902 |
| Chain | Residue |
| A | GLU270 |
| A | ASP353 |
| A | ASP360 |
| A | CYS471 |
| A | ASP474 |
| A | HOH5001 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 903 |
| Chain | Residue |
| A | GLU270 |
| A | ASP353 |
| A | ASP474 |
| A | HOH5013 |
| A | HOH5025 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 904 |
| Chain | Residue |
| A | ASP369 |
| A | LEU370 |
| A | CYS376 |
| A | THR378 |
| A | GLU398 |
| A | HOH5020 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE 097 B 801 |
| Chain | Residue |
| B | ASP377 |
| B | THR378 |
| B | LEU379 |
| B | GLY380 |
| B | HIS410 |
| B | GLU411 |
| B | HIS414 |
| B | HIS420 |
| B | SER440 |
| B | SER441 |
| B | ILE442 |
| B | LEU443 |
| B | ZN901 |
| B | HOH5012 |
| B | HOH5036 |
| B | HOH5179 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 901 |
| Chain | Residue |
| B | HIS410 |
| B | HIS414 |
| B | HIS420 |
| B | 097801 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 902 |
| Chain | Residue |
| B | GLU270 |
| B | ASP353 |
| B | ASP360 |
| B | CYS471 |
| B | ASP474 |
| B | HOH5006 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 903 |
| Chain | Residue |
| B | GLU270 |
| B | ASP353 |
| B | ASP474 |
| B | HOH5024 |
| B | HOH5071 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 904 |
| Chain | Residue |
| B | ASP369 |
| B | LEU370 |
| B | CYS376 |
| B | THR378 |
| B | GLU398 |
| B | HOH5019 |
Functional Information from PROSITE/UniProt
| site_id | PS00142 |
| Number of Residues | 10 |
| Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TVAHEIGHLL |
| Chain | Residue | Details |
| A | THR407-LEU416 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 418 |
| Details | Domain: {"description":"Peptidase M12B","evidences":[{"source":"PROSITE-ProRule","id":"PRU00276","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| 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_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18042673","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
