1GEE
Crystal structure of glucose dehydrogenase mutant Q252L complexed with NAD+
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 | 31 |
Details | BINDING SITE FOR RESIDUE NAD A 1262 |
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 | ILE195 |
A | ASN196 |
A | HOH1266 |
A | HOH1274 |
A | HOH1288 |
A | HOH1297 |
A | HOH1299 |
A | GLY18 |
A | HOH1305 |
A | HOH1372 |
A | LEU19 |
A | ARG39 |
A | GLY64 |
A | ASP65 |
A | VAL66 |
A | ASN92 |
site_id | AC2 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE NAD B 2262 |
Chain | Residue |
B | GLY14 |
B | THR17 |
B | GLY18 |
B | LEU19 |
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 | PRO194 |
B | ILE195 |
B | ASN196 |
B | HOH2264 |
B | HOH2281 |
B | HOH2282 |
B | HOH2322 |
B | HOH2325 |
B | HOH2332 |
site_id | AC3 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE NAD E 3262 |
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 | THR115 |
E | MET143 |
E | SER144 |
E | SER145 |
E | TYR158 |
E | LYS162 |
E | PRO188 |
E | GLY189 |
E | ILE191 |
E | THR193 |
E | PRO194 |
E | ILE195 |
E | ASN196 |
E | HOH3266 |
E | HOH3271 |
E | HOH3296 |
E | HOH3298 |
E | HOH3340 |
E | HOH3359 |
site_id | AC4 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE NAD F 4262 |
Chain | Residue |
F | GLY94 |
F | THR115 |
F | MET143 |
F | SER144 |
F | SER145 |
F | TYR158 |
F | LYS162 |
F | PRO188 |
F | GLY189 |
F | ILE191 |
F | THR193 |
F | PRO194 |
F | ILE195 |
F | ASN196 |
F | HOH4266 |
F | HOH4281 |
F | HOH4295 |
F | HOH4316 |
F | HOH4326 |
F | HOH4329 |
F | HOH4336 |
F | HOH4371 |
F | GLY14 |
F | THR17 |
F | GLY18 |
F | LEU19 |
F | GLY64 |
F | ASP65 |
F | VAL66 |
F | ASN92 |
F | ALA93 |
Functional Information from PROSITE/UniProt
site_id | PS00061 |
Number of Residues | 29 |
Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SvhekipwplFvhYAASKGGMkLMTeTLA |
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 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
A | SER145 | |
A | TYR158 | |
A | LYS162 |
site_id | CSA10 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
B | PHE155 | |
B | LYS162 |
site_id | CSA11 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
E | PHE155 | |
E | LYS162 |
site_id | CSA12 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
F | PHE155 | |
F | LYS162 |
site_id | CSA13 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
A | TYR158 | |
A | LYS162 |
site_id | CSA14 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
B | TYR158 | |
B | LYS162 |
site_id | CSA15 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
E | TYR158 | |
E | LYS162 |
site_id | CSA16 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
F | TYR158 | |
F | LYS162 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
B | SER145 | |
B | TYR158 | |
B | LYS162 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
E | SER145 | |
E | TYR158 | |
E | LYS162 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
F | SER145 | |
F | TYR158 | |
F | LYS162 |
site_id | CSA5 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
A | SER145 | |
A | TYR158 | |
A | ASN116 | |
A | LYS162 |
site_id | CSA6 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
B | SER145 | |
B | TYR158 | |
B | ASN116 | |
B | LYS162 |
site_id | CSA7 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
E | SER145 | |
E | TYR158 | |
E | ASN116 | |
E | LYS162 |
site_id | CSA8 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
F | SER145 | |
F | TYR158 | |
F | ASN116 | |
F | LYS162 |
site_id | CSA9 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
A | PHE155 | |
A | LYS162 |