1RWB
Cooperative Effect of Two Surface Amino Acid Mutations (Q252L and E170K) of Glucose Dehydrogenase from Bacillus megaterium IWG3 for the stabilization of Oligomeric State
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| A | 0047934 | molecular_function | glucose 1-dehydrogenase (NAD+) activity |
| A | 0047935 | molecular_function | glucose 1-dehydrogenase (NADP+) activity |
| A | 0047936 | molecular_function | glucose 1-dehydrogenase [NAD(P)] activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| B | 0047934 | molecular_function | glucose 1-dehydrogenase (NAD+) activity |
| B | 0047935 | molecular_function | glucose 1-dehydrogenase (NADP+) activity |
| B | 0047936 | molecular_function | glucose 1-dehydrogenase [NAD(P)] activity |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| E | 0047934 | molecular_function | glucose 1-dehydrogenase (NAD+) activity |
| E | 0047935 | molecular_function | glucose 1-dehydrogenase (NADP+) activity |
| E | 0047936 | molecular_function | glucose 1-dehydrogenase [NAD(P)] activity |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| F | 0047934 | molecular_function | glucose 1-dehydrogenase (NAD+) activity |
| F | 0047935 | molecular_function | glucose 1-dehydrogenase (NADP+) activity |
| F | 0047936 | molecular_function | glucose 1-dehydrogenase [NAD(P)] activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD A 601 |
| Chain | Residue |
| A | GLY14 |
| A | ALA93 |
| A | GLY94 |
| A | THR115 |
| A | MET143 |
| A | SER144 |
| A | SER145 |
| A | TYR158 |
| A | LYS162 |
| A | PRO188 |
| A | GLY189 |
| A | THR17 |
| A | ILE191 |
| A | THR193 |
| A | PRO194 |
| A | ASN196 |
| A | HOH602 |
| A | HOH649 |
| A | HOH712 |
| A | HOH736 |
| A | GLY18 |
| A | LEU19 |
| A | ARG39 |
| A | GLY64 |
| A | ASP65 |
| A | VAL66 |
| A | ASN92 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD B 701 |
| Chain | Residue |
| B | GLY14 |
| B | THR17 |
| B | GLY18 |
| B | LEU19 |
| B | ARG39 |
| B | GLY64 |
| B | ASP65 |
| B | VAL66 |
| B | ASN92 |
| B | ALA93 |
| B | GLY94 |
| B | THR115 |
| B | MET143 |
| B | SER144 |
| B | SER145 |
| B | TYR158 |
| B | LYS162 |
| B | PRO188 |
| B | GLY189 |
| B | ILE191 |
| B | THR193 |
| B | ILE195 |
| B | ASN196 |
| B | HOH708 |
| B | HOH769 |
| B | HOH805 |
| site_id | AC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD E 801 |
| Chain | Residue |
| E | GLY14 |
| E | THR17 |
| E | GLY18 |
| E | LEU19 |
| E | ARG39 |
| E | GLY64 |
| E | ASP65 |
| E | VAL66 |
| E | ASN92 |
| E | ALA93 |
| E | GLY94 |
| E | LEU95 |
| E | THR115 |
| E | MET143 |
| E | SER144 |
| E | SER145 |
| E | TYR158 |
| E | LYS162 |
| E | PRO188 |
| E | GLY189 |
| E | ILE191 |
| E | THR193 |
| E | ASN196 |
| E | HOH802 |
| E | HOH825 |
| E | HOH869 |
| site_id | AC4 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD F 901 |
| Chain | Residue |
| F | THR193 |
| F | PRO194 |
| F | ILE195 |
| F | ASN196 |
| F | HOH902 |
| F | HOH923 |
| F | HOH937 |
| F | HOH960 |
| F | HOH1030 |
| F | GLY14 |
| F | THR17 |
| F | GLY18 |
| F | LEU19 |
| F | ARG39 |
| F | GLY64 |
| F | ASP65 |
| F | VAL66 |
| F | ASN92 |
| F | ALA93 |
| F | GLY94 |
| F | THR115 |
| F | MET143 |
| F | SER144 |
| F | SER145 |
| F | TYR158 |
| F | LYS162 |
| F | PRO188 |
| F | GLY189 |
| F | ILE191 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SvhekipwplFvhYAASKGGMkLMTkTLA |
| Chain | Residue | Details |
| A | SER145-ALA173 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | TYR158 | |
| B | TYR158 | |
| E | TYR158 | |
| F | TYR158 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11173533 |
| Chain | Residue | Details |
| A | VAL11 | |
| B | VAL11 | |
| E | VAL11 | |
| F | VAL11 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | SER145 | |
| B | SER145 | |
| E | SER145 | |
| F | SER145 |
