Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 341 |
| Chain | Residue |
| B | ASN78 |
| B | VAL79 |
| B | GLY80 |
| B | TYR102 |
| B | ARG236 |
| B | HIS297 |
| B | NAD360 |
| B | HOH422 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD A 350 |
| Chain | Residue |
| A | ILE107 |
| A | GLY153 |
| A | GLY155 |
| A | HIS156 |
| A | ILE157 |
| A | TYR175 |
| A | ASP176 |
| A | ILE177 |
| A | HIS206 |
| A | VAL207 |
| A | PRO208 |
| A | ASN213 |
| A | VAL234 |
| A | SER235 |
| A | ARG236 |
| A | ASP260 |
| A | HIS297 |
| A | ALA299 |
| A | PHE300 |
| A | HOH390 |
| A | HOH428 |
| A | HOH463 |
| A | HOH470 |
| A | HOH485 |
| A | HOH487 |
| A | TYR102 |
| site_id | AC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD B 360 |
| Chain | Residue |
| B | TYR102 |
| B | ILE107 |
| B | GLY155 |
| B | HIS156 |
| B | ILE157 |
| B | TYR175 |
| B | ASP176 |
| B | ILE177 |
| B | HIS206 |
| B | VAL207 |
| B | PRO208 |
| B | ASN213 |
| B | VAL234 |
| B | SER235 |
| B | ARG236 |
| B | ASP260 |
| B | HIS297 |
| B | ALA299 |
| B | PHE300 |
| B | SO4341 |
| B | HOH376 |
| B | HOH379 |
| B | HOH382 |
| B | HOH386 |
| B | HOH395 |
| B | HOH453 |
Functional Information from PROSITE/UniProt
| site_id | PS00065 |
| Number of Residues | 28 |
| Details | D_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. VGVVGtGHIGqvfmqimegfgak.VItYD |
| Chain | Residue | Details |
| A | VAL149-ASP176 | |
| site_id | PS00670 |
| Number of Residues | 23 |
| Details | D_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. LYkqADVIsLHvPdvpaNvhMiN |
| Chain | Residue | Details |
| A | LEU196-ASN218 | |
| site_id | PS00671 |
| Number of Residues | 17 |
| Details | D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. MKqDvVIVNvSRGpLVD |
| Chain | Residue | Details |
| A | MET225-ASP241 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | ARG236 | |
| A | GLU265 | |
| B | ARG236 | |
| B | GLU265 | |
| Chain | Residue | Details |
| A | HIS297 | |
| B | HIS297 | |
| Chain | Residue | Details |
| A | HIS156 | |
| A | ASP176 | |
| A | ASN213 | |
| A | ASP260 | |
| B | HIS156 | |
| B | ASP176 | |
| B | ASN213 | |
| B | ASP260 | |
| Chain | Residue | Details |
| A | VAL207 | |
| B | VAL207 | |
| Chain | Residue | Details |
| A | VAL234 | |
| B | VAL234 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 12054772, 10712593 |
| Chain | Residue | Details |
| A | HIS297 | |
| A | ARG236 | |
| A | ASP260 | |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 576 |
| Chain | Residue | Details |
| A | ARG236 | electrostatic stabiliser |
| A | ASP260 | steric role |
| A | GLU265 | electrostatic stabiliser |
| A | HIS297 | proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 576 |
| Chain | Residue | Details |
| B | ARG236 | electrostatic stabiliser |
| B | ASP260 | steric role |
| B | GLU265 | electrostatic stabiliser |
| B | HIS297 | proton acceptor, proton donor |
