1OF0
CRYSTAL STRUCTURE OF BACILLUS SUBTILIS COTA AFTER 1H SOAKING WITH ABTS
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU1 A1511 |
| Chain | Residue |
| A | HIS419 |
| A | CYS492 |
| A | HIS497 |
| A | MET502 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU1 A1512 |
| Chain | Residue |
| A | HIS107 |
| A | HIS153 |
| A | HIS493 |
| A | OXY1515 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU1 A1513 |
| Chain | Residue |
| A | HIS422 |
| A | HIS424 |
| A | HIS491 |
| A | OXY1515 |
| A | HIS155 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE C1O A1514 |
| Chain | Residue |
| A | HIS105 |
| A | HIS107 |
| A | GLY108 |
| A | HIS422 |
| A | HIS424 |
| A | HOH2213 |
| A | HOH2235 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE OXY A1515 |
| Chain | Residue |
| A | HIS153 |
| A | HIS155 |
| A | HIS491 |
| A | HIS493 |
| A | GLU498 |
| A | CU11512 |
| A | CU11513 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE EBS A1518 |
| Chain | Residue |
| A | PRO226 |
| A | ALA227 |
| A | THR260 |
| A | GLY321 |
| A | CYS322 |
| A | GLY323 |
| A | LEU386 |
| A | THR415 |
| A | GLY417 |
| A | HIS419 |
| A | HIS497 |
| A | HOH2152 |
| A | HOH2238 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A1516 |
| Chain | Residue |
| A | ASP113 |
| A | ASP114 |
| A | TYR118 |
| A | ALA121 |
| A | TYR133 |
| A | LYS135 |
| A | HOH2236 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A1517 |
| Chain | Residue |
| A | ARG136 |
| A | GLU137 |
| A | VAL138 |
| A | PRO247 |
| A | THR307 |
| A | GLU310 |
| A | LEU343 |
| A | HOH2237 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| 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 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| 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 | |
| A | HIS153 | |
| A | HIS155 | |
| A | HIS424 | |
| A | HIS491 | |
| A | HIS493 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| 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 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| 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 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | SITE: Plays a crucial role in the protonation steps => ECO:0000305|PubMed:22481612 |
| Chain | Residue | Details |
| A | ASP116 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| 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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a65 |
| Chain | Residue | Details |
| A | HIS491 | |
| A | HIS493 | |
| A | CYS492 |
