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 | 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 | 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 | 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 |