MolNFT v1 · #13961 · protein
T and R states in the crystals of bacterial L-lactate dehydrogenase reveal the mechanism for allosteric control
1LTH · L-lactate dehydrogenase (T- and R- state tetramer complex): “T and R states in the crystals of bacterial L-lactate dehydrogenase reveal the mechanism for allosteric…”. X-ray diffraction, 3 ligands (FBP, NAD, OXM), 6 pockets (best…
- PDB
- 1LTH
- Type
- protein
- Length
- 626 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-lactate dehydrogenase (T- and R- state tetramer complex)
- EC
- 1.1.1.27
- UniProt
- P19869
- Ligands
- FBP, NAD, OXM
- Pockets
- 6 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| T, R | L-lactate dehydrogenase (T- and R- state tetramer complex) (EC 1.1.1.27) | protein | 313 | 47% helix, 19% strand | P19869 |
Ligands and binding sites
- FBP · 1,6-di-O-phosphono-beta-D-fructofuranose · ligand · 2 copies · chains T, R
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains T, R
- OXM · Oxamic acid · ligand · chains R
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 457 | 0.71 | 0.81 | 49 | NAD |
| 2 | 223 | 0.70 | 0.87 | 39 | NAD, OXM |
| 3 | 167 | 0.53 | 0.80 | 29 | empty |
| 4 | 176 | 0.45 | 0.74 | 31 | empty |
| 5 | 111 | 0.38 | 0.75 | 17 | empty |
Compared structures
- 1LTH · T and R states in the crystals of bacterial L-lactate dehydrogenase reveal the mechanism… · the same entry in another collection · chain T against T, 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 P19869
- Elsewhere: RCSB PDB 1LTH · PDBe 1LTH · UniProt P19869
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