5ZLJ
Crystal structure of CotA native enzyme, PH8.0
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 | HOH924 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue CU A 603 |
Chain | Residue |
A | HIS155 |
A | HIS422 |
A | HIS424 |
A | HIS491 |
A | HOH1086 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue CU A 604 |
Chain | Residue |
A | HIS107 |
A | HIS153 |
A | HIS493 |
A | HOH1086 |
site_id | AC5 |
Number of Residues | 8 |
Details | binding site for residue GOL A 605 |
Chain | Residue |
A | ASP113 |
A | ASP114 |
A | TYR118 |
A | ALA121 |
A | TYR133 |
A | LYS135 |
A | ARG487 |
A | HOH1040 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue EDO A 606 |
Chain | Residue |
A | GLU188 |
A | GLU244 |
A | TYR250 |
A | EDO610 |
A | HOH710 |
A | HOH741 |
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 | EDO609 |
A | HOH785 |
A | HOH799 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue EDO A 608 |
Chain | Residue |
A | ASP268 |
A | PRO328 |
A | ALA332 |
A | ASN333 |
A | HOH751 |
A | HOH841 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue EDO A 609 |
Chain | Residue |
A | HIS470 |
A | EDO607 |
A | HOH785 |
A | HOH988 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue EDO A 610 |
Chain | Residue |
A | GLU188 |
A | TYR189 |
A | GLU246 |
A | LYS341 |
A | EDO606 |
A | HOH749 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue EDO A 611 |
Chain | Residue |
A | ASP113 |
A | ASP114 |
A | LYS135 |
A | PRO342 |
A | LEU343 |
A | HOH804 |
site_id | AD3 |
Number of Residues | 8 |
Details | binding site for residue EDO A 612 |
Chain | Residue |
A | ARG136 |
A | GLU137 |
A | VAL138 |
A | PRO247 |
A | THR307 |
A | EDO613 |
A | HOH886 |
A | HOH1043 |
site_id | AD4 |
Number of Residues | 9 |
Details | binding site for residue EDO A 613 |
Chain | Residue |
A | TYR69 |
A | VAL138 |
A | THR307 |
A | ALA308 |
A | TYR309 |
A | GLU310 |
A | EDO612 |
A | HOH778 |
A | HOH978 |
site_id | AD5 |
Number of Residues | 8 |
Details | binding site for residue EDO A 614 |
Chain | Residue |
A | GLY108 |
A | ALA148 |
A | LEU150 |
A | ASP279 |
A | GLY280 |
A | SER427 |
A | ASP465 |
A | HOH892 |
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 |