Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008876 | molecular_function | quinoprotein glucose dehydrogenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0008876 | molecular_function | quinoprotein glucose dehydrogenase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 1001 |
| Chain | Residue |
| A | ALA269 |
| A | TYR271 |
| A | ASP273 |
| A | GLU309 |
| A | HOH1020 |
| A | HOH1056 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 1002 |
| Chain | Residue |
| A | HOH1042 |
| A | HOH1082 |
| A | HOH1215 |
| A | GLU253 |
| A | TYR263 |
| A | HOH1018 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 1003 |
| Chain | Residue |
| A | GLY247 |
| A | PRO248 |
| A | PQQ1004 |
| A | HOH1049 |
| A | HOH1198 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 1001 |
| Chain | Residue |
| B | ALA269 |
| B | TYR271 |
| B | ASP273 |
| B | GLU309 |
| B | HOH1028 |
| B | HOH1030 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 1002 |
| Chain | Residue |
| B | GLU253 |
| B | TYR263 |
| B | HOH1027 |
| B | HOH1040 |
| B | HOH1051 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 1003 |
| Chain | Residue |
| B | GLY247 |
| B | PRO248 |
| B | PQQ1004 |
| B | HOH1066 |
| B | HOH1297 |
| site_id | AC7 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PQQ A 1004 |
| Chain | Residue |
| A | GLN76 |
| A | HIS144 |
| A | ARG228 |
| A | ASN229 |
| A | GLN231 |
| A | GLN246 |
| A | GLY247 |
| A | PRO248 |
| A | TYR343 |
| A | TRP346 |
| A | THR348 |
| A | LEU376 |
| A | LYS377 |
| A | ARG406 |
| A | ARG408 |
| A | CA1003 |
| A | GOL1005 |
| A | HOH1178 |
| site_id | AC8 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE PQQ B 1004 |
| Chain | Residue |
| B | GLN76 |
| B | HIS144 |
| B | ARG228 |
| B | ASN229 |
| B | GLN231 |
| B | GLN246 |
| B | GLY247 |
| B | PRO248 |
| B | TYR343 |
| B | TRP346 |
| B | THR348 |
| B | LEU376 |
| B | LYS377 |
| B | ARG406 |
| B | ARG408 |
| B | CA1003 |
| B | GOL1005 |
| B | HOH1158 |
| B | HOH1240 |
| B | HOH1297 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 1005 |
| Chain | Residue |
| A | TYR343 |
| A | TRP346 |
| A | PQQ1004 |
| A | HOH1118 |
| A | HOH1198 |
| A | HOH1218 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 1005 |
| Chain | Residue |
| B | PQQ1004 |
| B | HOH1246 |
| B | HOH1253 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 1006 |
| Chain | Residue |
| A | GLN179 |
| A | HIS180 |
| A | THR181 |
| A | ASN216 |
| A | LYS299 |
| A | HOH1175 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 1007 |
| Chain | Residue |
| A | LEU4 |
| A | ASP335 |
| A | CYS345 |
| A | TRP346 |
| A | ARG378 |
| A | HOH1102 |
| A | HOH1122 |
| A | HOH1250 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | HIS144 | |
| B | HIS144 | |
| Chain | Residue | Details |
| A | GLN76 | |
| A | TYR271 | |
| A | ASP273 | |
| A | GLU309 | |
| A | TYR343 | |
| A | THR348 | |
| A | LYS377 | |
| B | GLN76 | |
| B | ASP143 | |
| B | GLN168 | |
| B | ARG228 | |
| A | ASP143 | |
| B | GLY247 | |
| B | PRO248 | |
| B | GLU253 | |
| B | TYR263 | |
| B | ALA269 | |
| B | TYR271 | |
| B | ASP273 | |
| B | GLU309 | |
| B | TYR343 | |
| B | THR348 | |
| A | GLN168 | |
| B | LYS377 | |
| A | ARG228 | |
| A | GLY247 | |
| A | PRO248 | |
| A | GLU253 | |
| A | TYR263 | |
| A | ALA269 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 10508152 |
| Chain | Residue | Details |
| A | HIS144 | |
| A | ASP163 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 10508152 |
| 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 |
