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 | 18 |
Details | BINDING SITE FOR RESIDUE NAI A 401 |
Chain | Residue |
A | THR154 |
A | ASN213 |
A | CYS234 |
A | SER235 |
A | ARG236 |
A | THR261 |
A | HIS297 |
A | ALA299 |
A | PHE337 |
A | OXM402 |
A | GLY155 |
A | HIS156 |
A | ILE157 |
A | ASP176 |
A | ILE177 |
A | HIS206 |
A | VAL207 |
A | PRO208 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE OXM A 402 |
Chain | Residue |
A | SER235 |
A | ARG236 |
A | HIS297 |
A | NAI401 |
site_id | AC3 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE NAI B 401 |
Chain | Residue |
B | THR154 |
B | GLY155 |
B | HIS156 |
B | ILE157 |
B | ASP176 |
B | ILE177 |
B | HIS206 |
B | VAL207 |
B | PRO208 |
B | ASN213 |
B | CYS234 |
B | SER235 |
B | ARG236 |
B | ASP260 |
B | THR261 |
B | HIS297 |
B | ALA299 |
B | OXM402 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE OXM B 402 |
Chain | Residue |
B | ARG236 |
B | HIS297 |
B | NAI401 |
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. VGVVGtGHIGqvfmrimegfgak.VIaYD |
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. MKdGvVIVNcSRGrLVD |
Chain | Residue | Details |
A | MET225-ASP241 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | GLY237 | |
A | VAL266 | |
B | GLY237 | |
B | VAL266 | |
Chain | Residue | Details |
A | THR298 | |
B | THR298 | |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000305|Ref.3 |
Chain | Residue | Details |
A | ILE157 | |
A | SER235 | |
B | ILE157 | |
B | SER235 | |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|Ref.3 |
Chain | Residue | Details |
A | ILE177 | |
A | PRO208 | |
A | VAL214 | |
A | THR261 | |
B | ILE177 | |
B | PRO208 | |
B | VAL214 | |
B | THR261 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1j49 |
Chain | Residue | Details |
A | ARG236 | |
A | ASP209 | |
A | GLU265 | |
A | HIS297 | |
A | ASP260 | |
site_id | CSA2 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1j49 |
Chain | Residue | Details |
B | ARG236 | |
B | ASP209 | |
B | GLU265 | |
B | HIS297 | |
B | ASP260 | |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1j49 |
Chain | Residue | Details |
A | GLU265 | |
A | HIS297 | |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1j49 |
Chain | Residue | Details |
B | GLU265 | |
B | HIS297 | |