Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008876 | molecular_function | quinoprotein glucose dehydrogenase activity |
| B | 0008876 | molecular_function | quinoprotein glucose dehydrogenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE PT B 462 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 463 |
| Chain | Residue |
| B | GLU253 |
| B | TYR263 |
| B | HOH470 |
| B | HOH473 |
| B | HOH483 |
| B | HOH493 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 464 |
| Chain | Residue |
| B | ASP273 |
| B | GLU309 |
| B | HOH480 |
| B | HOH999 |
| B | ALA269 |
| B | TYR271 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 465 |
| Chain | Residue |
| A | ALA269 |
| A | TYR271 |
| A | ASP273 |
| A | GLU309 |
| A | HOH486 |
| A | HOH875 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 466 |
| Chain | Residue |
| A | GLU253 |
| A | TYR263 |
| A | HOH487 |
| A | HOH500 |
| A | HOH504 |
| A | HOH521 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 467 |
| Chain | Residue |
| B | GLY247 |
| B | PRO248 |
| B | HOH533 |
| B | HOH572 |
| B | HOH592 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 468 |
| Chain | Residue |
| A | GLY247 |
| A | PRO248 |
| A | HOH520 |
| A | HOH664 |
| A | HOH672 |
| A | HOH870 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 469 |
| Chain | Residue |
| A | GLN39 |
| A | ARG52 |
| A | ASN54 |
| A | SER59 |
| A | LYS61 |
| B | LEU23 |
| B | GLY58 |
| B | HOH816 |
| B | HOH1076 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Region: {"description":"PQQ"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10508152","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1c9u |
| Chain | Residue | Details |
| A | HIS144 | |
| A | ASP163 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1c9u |
| Chain | Residue | Details |
| B | HIS144 | |
| B | ASP163 | |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 104 |
| Chain | Residue | Details |
| A | HIS144 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ASP163 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| A | ARG228 | electrostatic stabiliser, hydrogen bond donor |
| A | ALA269 | metal ligand |
| A | TYR271 | metal ligand |
| A | ASP273 | metal ligand |
| A | GLU309 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 104 |
| Chain | Residue | Details |
| B | HIS144 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ASP163 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| B | ARG228 | electrostatic stabiliser, hydrogen bond donor |
| B | ALA269 | metal ligand |
| B | TYR271 | metal ligand |
| B | ASP273 | metal ligand |
| B | GLU309 | metal ligand |
1QBI
