1ZXC
Crystal structure of catalytic domain of TNF-alpha converting enzyme (TACE) with 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 | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 201 |
| Chain | Residue |
| A | HIS405 |
| A | HIS409 |
| A | HIS415 |
| A | IH6478 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 202 |
| Chain | Residue |
| B | HIS405 |
| B | HIS409 |
| B | HIS415 |
| B | IH6478 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE IH6 A 478 |
| Chain | Residue |
| A | HOH56 |
| A | ZN201 |
| A | THR347 |
| A | LEU348 |
| A | GLY349 |
| A | LEU350 |
| A | LEU401 |
| A | VAL402 |
| A | HIS405 |
| A | GLU406 |
| A | HIS409 |
| A | HIS415 |
| A | VAL434 |
| A | PRO437 |
| A | VAL440 |
| A | HOH16 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE IH6 B 478 |
| Chain | Residue |
| B | HOH110 |
| B | ZN202 |
| B | GLU290 |
| B | GLY346 |
| B | THR347 |
| B | LEU348 |
| B | GLY349 |
| B | GLU398 |
| B | LEU401 |
| B | HIS405 |
| B | GLU406 |
| B | HIS409 |
| B | HIS415 |
| B | VAL434 |
| B | ALA439 |
| B | VAL440 |
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 | 502 |
| 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 |
