4AR8
Crystal structure of the peptidase domain of collagenase T from Clostridium tetani complexed with the peptidic inhibitor isoamyl- phosphonyl-Gly-Pro-Ala at 2.05 angstrom resolution.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004222 | molecular_function | metalloendopeptidase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0006508 | biological_process | proteolysis |
| A | 0008270 | molecular_function | zinc ion binding |
| B | 0004222 | molecular_function | metalloendopeptidase activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0006508 | biological_process | proteolysis |
| B | 0008270 | molecular_function | zinc ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1731 |
| Chain | Residue |
| A | HIS465 |
| A | HIS469 |
| A | GLU499 |
| C | IP80 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 1732 |
| Chain | Residue |
| A | HOH2055 |
| A | GLU440 |
| A | GLY473 |
| A | ILE477 |
| A | GLY479 |
| A | HOH2036 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1731 |
| Chain | Residue |
| B | HIS465 |
| B | HIS469 |
| B | GLU499 |
| D | IP80 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 1732 |
| Chain | Residue |
| B | GLU440 |
| B | GLY473 |
| B | ILE477 |
| B | GLY479 |
| B | HOH2027 |
| B | HOH2045 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR CHAIN C OF ISOAMYL-PHOSPHONYL-GLY-PRO-ALA |
| Chain | Residue |
| A | GLY435 |
| A | GLY436 |
| A | SER455 |
| A | TYR457 |
| A | LEU462 |
| A | HIS465 |
| A | GLU466 |
| A | HIS469 |
| A | GLU499 |
| A | GLU503 |
| A | TRP545 |
| A | TYR548 |
| A | ZN1731 |
| A | HOH2050 |
| A | HOH2051 |
| A | HOH2056 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR CHAIN D OF ISOAMYL-PHOSPHONYL-GLY-PRO-ALA |
| Chain | Residue |
| B | ASN434 |
| B | GLY435 |
| B | GLY436 |
| B | ILE437 |
| B | TYR438 |
| B | SER455 |
| B | TYR457 |
| B | LEU462 |
| B | HIS465 |
| B | GLU466 |
| B | HIS469 |
| B | GLU499 |
| B | GLU503 |
| B | TRP545 |
| B | TYR548 |
| B | ZN1731 |
| B | HOH2048 |
Functional Information from PROSITE/UniProt
| site_id | PS00142 |
| Number of Residues | 10 |
| Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. LFRHEFTHYL |
| Chain | Residue | Details |
| A | LEU462-LEU471 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 271 |
| Details | Region: {"description":"Catalytic subdomain","evidences":[{"source":"PubMed","id":"23703618","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23703618","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4AR8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4AR9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23703618","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4AR8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4AR9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
