2YQ5
Crystal Structure of D-isomer specific 2-hydroxyacid dehydrogenase from Lactobacillus delbrueckii ssp. bulgaricus: NAD complexed form
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0008720 | molecular_function | D-lactate dehydrogenase activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0051287 | molecular_function | NAD binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0008720 | molecular_function | D-lactate dehydrogenase activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
B | 0051287 | molecular_function | NAD binding |
C | 0000166 | molecular_function | nucleotide binding |
C | 0008720 | molecular_function | D-lactate dehydrogenase activity |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
C | 0051287 | molecular_function | NAD binding |
D | 0000166 | molecular_function | nucleotide binding |
D | 0008720 | molecular_function | D-lactate dehydrogenase activity |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE NAD A 0 |
Chain | Residue |
A | ILE107 |
A | HIS207 |
A | THR208 |
A | PRO209 |
A | CYS235 |
A | ALA236 |
A | ARG237 |
A | ASP261 |
A | HIS298 |
A | ALA300 |
A | PHE301 |
A | VAL156 |
A | GLY157 |
A | HIS158 |
A | ILE159 |
A | TYR177 |
A | ASP178 |
A | VAL179 |
A | ALA180 |
site_id | AC2 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE NAD B 0 |
Chain | Residue |
B | TYR102 |
B | ILE107 |
B | GLY155 |
B | VAL156 |
B | GLY157 |
B | HIS158 |
B | ILE159 |
B | TYR177 |
B | ASP178 |
B | VAL179 |
B | ALA180 |
B | HIS207 |
B | THR208 |
B | PRO209 |
B | CYS235 |
B | ALA236 |
B | ARG237 |
B | ASP261 |
B | HIS298 |
B | ALA300 |
B | PHE301 |
site_id | AC3 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE NAD C 0 |
Chain | Residue |
C | TYR102 |
C | ILE107 |
C | GLY155 |
C | VAL156 |
C | GLY157 |
C | HIS158 |
C | ILE159 |
C | TYR177 |
C | ASP178 |
C | VAL179 |
C | ALA180 |
C | HIS207 |
C | THR208 |
C | PRO209 |
C | CYS235 |
C | ALA236 |
C | ARG237 |
C | ASP261 |
C | HIS298 |
C | ALA300 |
C | PHE301 |
C | HOH2001 |
site_id | AC4 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE NAD D 0 |
Chain | Residue |
D | TYR102 |
D | ILE107 |
D | GLY155 |
D | VAL156 |
D | GLY157 |
D | HIS158 |
D | ILE159 |
D | TYR177 |
D | ASP178 |
D | ALA180 |
D | HIS207 |
D | THR208 |
D | PRO209 |
D | MET217 |
D | CYS235 |
D | ARG237 |
D | ASP261 |
D | HIS298 |
D | ALA300 |
D | PHE301 |
Functional Information from PROSITE/UniProt
site_id | PS00670 |
Number of Residues | 23 |
Details | D_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. VLkeADIVsLHtPlfpsTenMiG |
Chain | Residue | Details |
A | VAL197-GLY219 |
site_id | PS00671 |
Number of Residues | 17 |
Details | D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. MKkSaYLINcARGeLVD |
Chain | Residue | Details |
A | MET226-ASP242 |