3AY6
Crystal structure of Bacillus megaterium glucose dehydrogenase 4 A258F mutant in complex with NADH and D-glucose
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042802 | molecular_function | identical protein binding |
| 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 | 0000166 | molecular_function | nucleotide binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042802 | molecular_function | identical protein binding |
| 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 |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0047934 | molecular_function | glucose 1-dehydrogenase (NAD+) activity |
| C | 0047935 | molecular_function | glucose 1-dehydrogenase (NADP+) activity |
| C | 0047936 | molecular_function | glucose 1-dehydrogenase [NAD(P)+] activity |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0047934 | molecular_function | glucose 1-dehydrogenase (NAD+) activity |
| D | 0047935 | molecular_function | glucose 1-dehydrogenase (NADP+) activity |
| D | 0047936 | molecular_function | glucose 1-dehydrogenase [NAD(P)+] activity |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SvhemipwplFvhYAASKGGMkLMTeTLA |
| Chain | Residue | Details |
| A | SER145-ALA173 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10001","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 40 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22804868","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3AUT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AY6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22804868","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3AUU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AY6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22804868","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3AY6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
