Research workbench
Plasmodium falciparum lactate dehydrogenase complexed with NAD+ and 4- hydroxy-1,2,5-oxadiazole-3-carboxylic acid
Analyse Plasmodium falciparum lactate dehydrogenase complexed with NAD+ and 4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1T24
- Type
- protein
- Length
- 315 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-lactate dehydrogenase
- EC
- 1.1.1.27
- UniProt
- Q27743
- Ligands
- NAD, OXQ
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-lactate dehydrogenase (EC 1.1.1.27) | protein | 315 | 50% helix, 20% strand | Q27743 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A
- OXQ · 4-hydroxy-1,2,5-oxadiazole-3-carboxylic acid · ligand · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 248 | 0.69 | 0.84 | 39 | NAD, OXQ |
| 2 | 117 | 0.43 | 0.77 | 22 | GOL |
| 3 | 52 | 0.25 | 0.72 | 13 | empty |
Compared structures
- 1T24 · Plasmodium falciparum lactate dehydrogenase complexed with NAD+ and… · the same entry in another collection · chain A against A, TM-score 1.00
- Q27743 · AlphaFold monomer V2.0 prediction for L-lactate dehydrogenase (Q27743) · a predicted model of the same protein · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q27743
- Elsewhere: RCSB PDB 1T24 · PDBe 1T24 · UniProt Q27743
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