3EDZ
Crystal structure of catalytic domain of TACE with hydroxamate 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 |
| 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 | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 1 |
| Chain | Residue |
| A | INN2 |
| A | HIS405 |
| A | HIS409 |
| A | HIS415 |
| A | HOH648 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE INN A 2 |
| Chain | Residue |
| A | MET345 |
| A | GLY346 |
| A | THR347 |
| A | LEU348 |
| A | GLY349 |
| A | ASN389 |
| A | TYR390 |
| A | HIS405 |
| A | GLU406 |
| A | HIS409 |
| A | HIS415 |
| A | PRO437 |
| A | ILE438 |
| A | ALA439 |
| A | HOH508 |
| A | HOH614 |
| A | HOH648 |
| A | HOH651 |
| A | ZN1 |
| A | GLU327 |
| A | SER330 |
| A | LYS331 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE CIT A 4 |
| Chain | Residue |
| A | GLY353 |
| A | SER355 |
| A | SER360 |
| A | HIS361 |
| A | GLY362 |
| A | LYS367 |
| A | LYS465 |
| A | HOH520 |
| A | HOH522 |
| A | HOH529 |
| A | HOH531 |
| A | HOH642 |
| A | HOH664 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 2 |
| Chain | Residue |
| B | 5501 |
| B | HIS405 |
| B | HIS409 |
| B | HIS415 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE 550 B 1 |
| Chain | Residue |
| B | ZN2 |
| B | GLY346 |
| B | THR347 |
| B | LEU348 |
| B | GLY349 |
| B | LEU401 |
| B | HIS405 |
| B | GLU406 |
| B | HIS409 |
| B | HIS415 |
| B | VAL434 |
| B | TYR436 |
| B | PRO437 |
| B | ALA439 |
| B | VAL440 |
| B | SER441 |
| B | GLY442 |
| B | HOH827 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CIT B 3 |
| Chain | Residue |
| A | PRO356 |
| A | ARG357 |
| A | HIS415 |
| A | PRO437 |
| A | HOH650 |
| B | ARG357 |
| B | ASN359 |
| B | SER360 |
| B | HIS361 |
| B | HOH728 |
| B | HOH736 |
| B | HOH857 |
Functional Information from PROSITE/UniProt
| site_id | PS00142 |
| Number of Residues | 10 |
| Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VTTHELGHNF |
| Chain | Residue | Details |
| A | VAL402-PHE411 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 251 |
| 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":"9520379","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9520379","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
