Research workbench
Structure determination of the allosteric L-lactate dehydrogenase from lactobacillus casei at 3.0 ångströms resolution
Analyse Structure determination of the allosteric L-lactate dehydrogenase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LLC
- Type
- protein
- Length
- 320 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
- P00343
- Ligands
- AFP, SO4
- Pockets
- 4 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-lactate dehydrogenase (EC 1.1.1.27) | protein | 320 | 27% helix, 14% strand | P00343 |
Ligands and binding sites
- AFP · 1,6-di-O-phosphono-alpha-D-fructofuranose · ligand · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 323 | 0.67 | 0.82 | 53 | SO4 |
| 2 | 197 | 0.54 | 0.78 | 34 | empty |
| 3 | 149 | 0.47 | 0.77 | 20 | AFP |
| 4 | 54 | 0.34 | 0.78 | 14 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 1LLC · Structure determination of the allosteric L-lactate dehydrogenase from lactobacillus… · the same entry in another collection · chain A against A, TM-score 1.00
- P00343 · AlphaFold monomer V2.0 prediction for L-lactate dehydrogenase (P00343) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 P00343
- Elsewhere: RCSB PDB 1LLC · PDBe 1LLC · UniProt P00343
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