3LQF
Crystal structure of the short-chain dehydrogenase Galactitol-Dehydrogenase (GatDH) of Rhodobacter sphaeroides in complex with NAD and erythritol
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0046872 | molecular_function | metal ion binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
B | 0046872 | molecular_function | metal ion binding |
C | 0000166 | molecular_function | nucleotide binding |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
C | 0046872 | molecular_function | metal ion binding |
D | 0000166 | molecular_function | nucleotide binding |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 255 |
Chain | Residue |
A | TRP254 |
A | HOH317 |
A | HOH336 |
A | HOH344 |
B | TRP254 |
B | HOH301 |
site_id | AC2 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE NAD A 257 |
Chain | Residue |
A | ILE23 |
A | ASP42 |
A | ARG43 |
A | ALA65 |
A | ASP66 |
A | VAL67 |
A | SER92 |
A | LEU142 |
A | GLY143 |
A | SER144 |
A | TYR159 |
A | LYS163 |
A | PRO189 |
A | GLY190 |
A | VAL192 |
A | THR194 |
A | GLU195 |
A | MET196 |
A | THR197 |
A | MRY258 |
A | HOH324 |
A | HOH334 |
A | HOH424 |
A | HOH436 |
A | GLY18 |
A | SER21 |
A | GLY22 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MRY A 258 |
Chain | Residue |
A | ALA96 |
A | ASN151 |
A | GLN154 |
A | TYR191 |
A | THR197 |
A | MET200 |
A | NAD257 |
A | HOH436 |
site_id | AC4 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE NAD B 257 |
Chain | Residue |
B | SER21 |
B | GLY22 |
B | ILE23 |
B | ASP42 |
B | ARG43 |
B | GLU44 |
B | ALA65 |
B | ASP66 |
B | VAL67 |
B | SER92 |
B | ALA93 |
B | GLY94 |
B | LEU142 |
B | GLY143 |
B | SER144 |
B | TYR159 |
B | LYS163 |
B | GLY190 |
B | VAL192 |
B | THR194 |
B | MET196 |
B | THR197 |
B | MRY258 |
B | HOH319 |
B | HOH371 |
B | HOH399 |
B | HOH419 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MRY B 258 |
Chain | Residue |
B | ALA96 |
B | LEU98 |
B | GLN154 |
B | TYR159 |
B | TYR191 |
B | NAD257 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG C 255 |
Chain | Residue |
C | TRP254 |
C | HOH339 |
D | TRP254 |
D | HOH307 |
D | HOH327 |
D | HOH339 |
site_id | AC7 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE NAD C 257 |
Chain | Residue |
C | MET196 |
C | THR197 |
C | MRY258 |
C | HOH360 |
C | HOH369 |
C | HOH415 |
C | HOH416 |
C | SER21 |
C | GLY22 |
C | ILE23 |
C | ASP42 |
C | ARG43 |
C | ALA65 |
C | ASP66 |
C | VAL67 |
C | SER92 |
C | GLY94 |
C | LEU142 |
C | GLY143 |
C | SER144 |
C | TYR159 |
C | LYS163 |
C | PRO189 |
C | GLY190 |
C | VAL192 |
C | THR194 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MRY C 258 |
Chain | Residue |
C | GLN154 |
C | TYR159 |
C | MET196 |
C | THR197 |
C | MET200 |
C | NAD257 |
C | HOH416 |
site_id | AC9 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE NAD D 257 |
Chain | Residue |
D | SER21 |
D | GLY22 |
D | ILE23 |
D | ASP42 |
D | ARG43 |
D | ALA65 |
D | ASP66 |
D | VAL67 |
D | SER92 |
D | ALA93 |
D | GLY94 |
D | LEU142 |
D | GLY143 |
D | SER144 |
D | TYR159 |
D | LYS163 |
D | GLY190 |
D | VAL192 |
D | THR194 |
D | MET196 |
D | THR197 |
D | MRY258 |
D | HOH326 |
D | HOH363 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MRY D 258 |
Chain | Residue |
D | GLN154 |
D | NAD257 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:20410293 |
Chain | Residue | Details |
A | TYR159 | |
B | TYR159 | |
C | TYR159 | |
D | TYR159 |
site_id | SWS_FT_FI2 |
Number of Residues | 28 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20410293, ECO:0007744|PDB:2WDZ, ECO:0007744|PDB:2WSB, ECO:0007744|PDB:3LQF |
Chain | Residue | Details |
A | SER21 | |
B | ASP66 | |
B | TYR159 | |
B | LYS163 | |
B | VAL192 | |
B | TRP254 | |
C | SER21 | |
C | ASP42 | |
C | ASP66 | |
C | TYR159 | |
C | LYS163 | |
A | ASP42 | |
C | VAL192 | |
C | TRP254 | |
D | SER21 | |
D | ASP42 | |
D | ASP66 | |
D | TYR159 | |
D | LYS163 | |
D | VAL192 | |
D | TRP254 | |
A | ASP66 | |
A | TYR159 | |
A | LYS163 | |
A | VAL192 | |
A | TRP254 | |
B | SER21 | |
B | ASP42 |