2BHF
3D structure of the reduced form of CotA
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 A1512 |
Chain | Residue |
A | HIS419 |
A | CYS492 |
A | HIS497 |
A | MET502 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CU1 A1513 |
Chain | Residue |
A | HIS107 |
A | HIS153 |
A | HIS493 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU1 A1514 |
Chain | Residue |
A | VAL489 |
A | HIS491 |
A | HIS155 |
A | HIS424 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CU1 A1515 |
Chain | Residue |
A | HIS105 |
A | HIS107 |
A | HIS422 |
A | HIS424 |
A | HOH2099 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A1516 |
Chain | Residue |
A | ASP113 |
A | ASP114 |
A | TYR118 |
A | ALA121 |
A | TYR133 |
A | LYS135 |
A | HOH2121 |
A | HOH2127 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A1517 |
Chain | Residue |
A | LYS25 |
A | VAL138 |
A | THR307 |
A | ALA308 |
A | TYR309 |
A | GLU310 |
A | GOL1518 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A1518 |
Chain | Residue |
A | ARG136 |
A | GLU137 |
A | VAL138 |
A | THR307 |
A | GLU310 |
A | GOL1517 |
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 |