5ZLM
Mutation in the trinuclear site of CotA-laccase: H491C mutant, PH 8.0
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 CU A 601 |
| Chain | Residue |
| A | HIS419 |
| A | CYS492 |
| A | HIS497 |
| A | MET502 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue CU A 602 |
| Chain | Residue |
| A | HIS105 |
| A | HIS107 |
| A | HIS422 |
| A | HIS424 |
| A | HOH932 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue CU A 603 |
| Chain | Residue |
| A | HIS107 |
| A | HIS153 |
| A | HIS493 |
| A | HOH1168 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 604 |
| Chain | Residue |
| A | ASP113 |
| A | ASP114 |
| A | TYR118 |
| A | ALA121 |
| A | TYR133 |
| A | LYS135 |
| A | ARG487 |
| A | EDO613 |
| A | HOH806 |
| A | HOH1055 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 605 |
| Chain | Residue |
| A | ASN75 |
| A | LEU76 |
| A | PRO77 |
| A | LYS125 |
| A | GLN367 |
| A | ASN368 |
| A | HOH741 |
| A | HOH764 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 606 |
| Chain | Residue |
| A | GLU188 |
| A | GLU244 |
| A | TYR250 |
| A | HOH712 |
| A | HOH721 |
| A | HOH1106 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 607 |
| Chain | Residue |
| A | PHE292 |
| A | SER293 |
| A | TYR300 |
| A | PRO457 |
| A | SER459 |
| A | HOH780 |
| A | HOH977 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 608 |
| Chain | Residue |
| A | ASP268 |
| A | ALA317 |
| A | PRO328 |
| A | ASN333 |
| A | HOH723 |
| A | HOH727 |
| A | HOH994 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 609 |
| Chain | Residue |
| A | GLY108 |
| A | ALA148 |
| A | LEU150 |
| A | ASP279 |
| A | GLY280 |
| A | SER427 |
| A | ASP465 |
| A | HOH896 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 610 |
| Chain | Residue |
| A | ASN74 |
| A | LEU76 |
| A | PRO77 |
| A | SER78 |
| A | VAL100 |
| A | SER124 |
| A | LYS125 |
| A | HOH1140 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 611 |
| Chain | Residue |
| A | LYS25 |
| A | TYR69 |
| A | THR307 |
| A | ALA308 |
| A | TYR309 |
| A | GLU310 |
| A | HOH918 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 612 |
| Chain | Residue |
| A | ARG136 |
| A | GLU137 |
| A | VAL138 |
| A | PRO247 |
| A | LEU343 |
| A | HOH742 |
| A | HOH1065 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 613 |
| Chain | Residue |
| A | ASP113 |
| A | ASP114 |
| A | LYS135 |
| A | LEU343 |
| A | GOL604 |
| A | EDO614 |
| A | HOH788 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 614 |
| Chain | Residue |
| A | PRO112 |
| A | ASP113 |
| A | TYR484 |
| A | SER485 |
| A | TYR488 |
| A | EDO613 |
| A | HOH749 |
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 | HIS424 | |
| A | CYS491 | |
| A | HIS493 | |
| A | HIS107 | |
| A | HIS153 | |
| A | HIS155 |
| 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 |
