7JP2
Crystal structure of TP0037 from Treponema pallidum, a D-lactate dehydrogenase
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 | 5 |
| Details | binding site for residue EDO A 401 |
| Chain | Residue |
| A | PHE54 |
| A | THR77 |
| A | TYR101 |
| A | HOH701 |
| B | TRP135 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 402 |
| Chain | Residue |
| B | ARG9 |
| B | GLU11 |
| A | TRP135 |
| A | GLN136 |
| A | LYS137 |
| A | HOH618 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 403 |
| Chain | Residue |
| A | THR303 |
| A | HOH543 |
| B | GLU143 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 401 |
| Chain | Residue |
| A | TRP135 |
| B | THR77 |
| B | TYR101 |
| B | HOH667 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 402 |
| Chain | Residue |
| B | LEU117 |
| B | GLU123 |
| B | TYR229 |
| B | ALA254 |
| B | GLY255 |
| B | ARG290 |
| B | HOH549 |
| B | HOH556 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 403 |
| Chain | Residue |
| A | ARG131 |
| A | PHE263 |
| A | HOH568 |
| B | ASN272 |
| B | GLY273 |
| B | ASN275 |
| B | PRO276 |
| B | ILE277 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 404 |
| Chain | Residue |
| A | GLU125 |
| A | VAL128 |
| B | ARG122 |
| B | ILE291 |
| B | ILE292 |
| B | TYR293 |
| B | HOH586 |
| B | HOH594 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 405 |
| Chain | Residue |
| A | GLU143 |
| B | GLU302 |
| B | THR303 |
| B | HOH560 |
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. VGILGtGRIGqaaarlfkgvgaq.VVgFD |
| 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. LLstSDVIsLHmPatkdShhLiN |
| Chain | Residue | Details |
| A | LEU195-ASN217 |
| site_id | PS00671 |
| Number of Residues | 17 |
| Details | D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. MKdGvYLVNtARGaVID |
| Chain | Residue | Details |
| A | MET224-ASP240 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P26297 |
| Chain | Residue | Details |
| A | ARG235 | |
| A | GLU264 | |
| B | ARG235 | |
| B | GLU264 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P26297 |
| Chain | Residue | Details |
| A | HIS296 | |
| B | HIS296 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P30901 |
| Chain | Residue | Details |
| A | ARG156 | |
| A | MET206 | |
| A | THR233 | |
| A | ASP259 | |
| B | ARG156 | |
| B | MET206 | |
| B | THR233 | |
| B | ASP259 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P26297 |
| Chain | Residue | Details |
| A | ASP176 | |
| B | ASP176 |
