7Y8C
Crystal structure of CotA laccase complexed with syringaldehyde
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| B | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: type 2 copper site => ECO:0000269|PubMed:12637519, ECO:0000269|PubMed:14764581, ECO:0000269|PubMed:16234932, ECO:0000269|PubMed:20822511, ECO:0007744|PDB:1GSK, ECO:0007744|PDB:1OF0, ECO:0007744|PDB:1W6L, ECO:0007744|PDB:1W6W, ECO:0007744|PDB:1W8E, ECO:0007744|PDB:2BHF, ECO:0007744|PDB:2X87, ECO:0007744|PDB:2X88, ECO:0007744|PDB:3ZDW |
| Chain | Residue | Details |
| A | HIS105 | |
| A | HIS422 | |
| B | HIS105 | |
| B | HIS422 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: type 3 copper site => ECO:0000269|PubMed:12637519, ECO:0000269|PubMed:14764581, ECO:0000269|PubMed:16234932, ECO:0000269|PubMed:20822511, ECO:0000269|PubMed:27050268, ECO:0007744|PDB:1GSK, ECO:0007744|PDB:1OF0, ECO:0007744|PDB:1W6L, ECO:0007744|PDB:1W6W, ECO:0007744|PDB:1W8E, ECO:0007744|PDB:2BHF, ECO:0007744|PDB:2X87, ECO:0007744|PDB:2X88, ECO:0007744|PDB:3ZDW, ECO:0007744|PDB:4YVN, ECO:0007744|PDB:4YVU |
| Chain | Residue | Details |
| A | HIS107 | |
| B | HIS424 | |
| B | HIS491 | |
| B | HIS493 | |
| A | HIS153 | |
| A | HIS155 | |
| A | HIS424 | |
| A | HIS491 | |
| A | HIS493 | |
| B | HIS107 | |
| B | HIS153 | |
| B | HIS155 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: type 1 copper site => ECO:0000269|PubMed:12637519, ECO:0000269|PubMed:14764581, ECO:0000269|PubMed:16234932, ECO:0000269|PubMed:20822511, ECO:0000269|PubMed:27050268, ECO:0007744|PDB:1GSK, ECO:0007744|PDB:1OF0, ECO:0007744|PDB:1W6L, ECO:0007744|PDB:1W6W, ECO:0007744|PDB:1W8E, ECO:0007744|PDB:2BHF, ECO:0007744|PDB:2X87, ECO:0007744|PDB:2X88, ECO:0007744|PDB:3ZDW, ECO:0007744|PDB:4YVN, ECO:0007744|PDB:4YVU |
| Chain | Residue | Details |
| A | HIS419 | |
| A | CYS492 | |
| A | HIS497 | |
| B | HIS419 | |
| B | CYS492 | |
| B | HIS497 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: type 1 copper site => ECO:0000269|PubMed:12637519, ECO:0000269|PubMed:16234932, ECO:0000269|PubMed:20822511, ECO:0000269|PubMed:27050268, ECO:0007744|PDB:1GSK, ECO:0007744|PDB:1OF0, ECO:0007744|PDB:1W6L, ECO:0007744|PDB:1W8E, ECO:0007744|PDB:2BHF, ECO:0007744|PDB:2X87, ECO:0007744|PDB:2X88, ECO:0007744|PDB:4YVN, ECO:0007744|PDB:4YVU |
| Chain | Residue | Details |
| A | MET502 | |
| B | MET502 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Plays a crucial role in the protonation steps => ECO:0000305|PubMed:22481612 |
| Chain | Residue | Details |
| A | ASP116 | |
| B | ASP116 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | SITE: Plays a crucial role in the protonation steps => ECO:0000305|PubMed:20200715, ECO:0000305|PubMed:20822511, ECO:0000305|PubMed:22481612 |
| Chain | Residue | Details |
| A | GLU498 | |
| B | GLU498 |
