4Q8B
The crystal structure of CotA laccase complexed with sinapic acid
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 PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU A 601 |
| Chain | Residue |
| A | HIS419 |
| A | CYS492 |
| A | HIS497 |
| A | MET502 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CU A 602 |
| Chain | Residue |
| A | HOH741 |
| A | HIS105 |
| A | HIS107 |
| A | HIS422 |
| A | HIS424 |
| A | OXY605 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU A 603 |
| Chain | Residue |
| A | HIS155 |
| A | HIS424 |
| A | HIS491 |
| A | OXY605 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU A 604 |
| Chain | Residue |
| A | HIS107 |
| A | HIS153 |
| A | HIS493 |
| A | OXY605 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE OXY A 605 |
| Chain | Residue |
| A | HIS105 |
| A | HIS107 |
| A | HIS153 |
| A | HIS155 |
| A | HIS422 |
| A | HIS424 |
| A | HIS491 |
| A | HIS493 |
| A | CU602 |
| A | CU603 |
| A | CU604 |
| A | HOH1144 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 607 |
| Chain | Residue |
| A | SER186 |
| A | ARG248 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 608 |
| Chain | Residue |
| A | ASN264 |
| A | SER293 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 609 |
| Chain | Residue |
| A | HOH1146 |
| A | HOH1147 |
| A | HOH1150 |
| A | HOH1151 |
| A | HOH1152 |
| A | HOH1153 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 610 |
| Chain | Residue |
| A | HOH751 |
| A | HOH986 |
| A | HOH1108 |
| A | HOH1154 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU B 601 |
| Chain | Residue |
| B | HIS419 |
| B | CYS492 |
| B | HIS497 |
| B | MET502 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CU B 602 |
| Chain | Residue |
| B | HIS105 |
| B | HIS107 |
| B | HIS422 |
| B | HIS424 |
| B | CU603 |
| B | HOH721 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU B 603 |
| Chain | Residue |
| B | HIS155 |
| B | HIS424 |
| B | HIS491 |
| B | CU602 |
| B | HOH701 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU B 604 |
| Chain | Residue |
| B | HIS107 |
| B | HIS153 |
| B | HIS493 |
| B | HOH701 |
| site_id | BC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SXX B 605 |
| Chain | Residue |
| B | PRO226 |
| B | GLY376 |
| B | THR377 |
| B | LEU386 |
| B | THR415 |
| B | ARG416 |
| B | GLY417 |
| B | HOH774 |
| B | HOH945 |
| B | HOH1074 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PGE B 606 |
| Chain | Residue |
| B | LYS25 |
| B | TYR27 |
| B | TYR69 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 607 |
| Chain | Residue |
| B | GLY376 |
| B | GLN442 |
| B | HOH945 |
| site_id | BC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 608 |
| Chain | Residue |
| B | GLY404 |
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 |
