3ZDW
Substrate and dioxygen binding to the endospore coat laccase CotA from Bacillus subtilis
Replaces: 1UVWFunctional 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 A 1511 |
Chain | Residue |
A | HIS419 |
A | CYS492 |
A | HIS497 |
A | MET502 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU1 A 1512 |
Chain | Residue |
A | HIS107 |
A | HIS153 |
A | HIS493 |
A | OXY1515 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CU1 A 1513 |
Chain | Residue |
A | HIS424 |
A | HIS491 |
A | CU11514 |
A | OXY1515 |
A | HIS155 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CU1 A 1514 |
Chain | Residue |
A | HIS105 |
A | HIS107 |
A | HIS422 |
A | HIS424 |
A | CU11513 |
A | OXY1515 |
A | HOH2056 |
site_id | AC5 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE OXY A 1515 |
Chain | Residue |
A | HIS105 |
A | HIS107 |
A | HIS153 |
A | HIS155 |
A | HIS422 |
A | HIS424 |
A | HIS491 |
A | HIS493 |
A | CU11512 |
A | CU11513 |
A | CU11514 |
A | HOH2093 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EBS A 1516 |
Chain | Residue |
A | PRO226 |
A | ALA227 |
A | CYS229 |
A | GLY323 |
A | PRO384 |
A | HIS497 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 1519 |
Chain | Residue |
A | ASP113 |
A | ASP114 |
A | TYR133 |
A | LYS135 |
A | ARG487 |
A | HOH2062 |
A | HOH2064 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 1520 |
Chain | Residue |
A | ARG136 |
A | GLU137 |
A | VAL138 |
A | PRO247 |
A | THR307 |
A | GLU310 |
A | GOL1524 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 1521 |
Chain | Residue |
A | GLN20 |
A | LYS25 |
A | VAL138 |
A | ALA308 |
A | GLU310 |
A | GOL1524 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 1522 |
Chain | Residue |
A | PRO112 |
A | ASP113 |
A | TYR484 |
A | SER485 |
A | TYR488 |
A | HOH2069 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 1523 |
Chain | Residue |
A | GLU128 |
A | ILE369 |
A | THR371 |
A | SER410 |
A | ARG476 |
A | GOL1525 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 1524 |
Chain | Residue |
A | VAL138 |
A | THR307 |
A | ALA308 |
A | TYR309 |
A | GLU310 |
A | GOL1520 |
A | GOL1521 |
site_id | BC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL A 1525 |
Chain | Residue |
A | LEU447 |
A | GOL1523 |
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 |