Research workbench
Plasmodium falciparum lactate dehydrogenase complexed with 2-({4- chloro-[HYDROXY(METHOXY)METHYL]CYCLOHEXYL}AMINO)ETHANE-1,1,2-triol
Analyse Plasmodium falciparum lactate dehydrogenase complexed with 2-({4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1XIV
- Type
- protein
- Length
- 307 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
- RB2
- Pockets
- 3 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-lactate dehydrogenase (EC 1.1.1.27) | protein | 307 | 49% helix, 21% strand | Q27743 |
Ligands and binding sites
- RB2 · 2-({4-chloro-2-[hydroxy(methoxy)methyl]cyclohexyl}amino)ethane-1,1,2-triol · 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 | 475 | 0.63 | 0.76 | 58 | RB2 |
| 2 | 130 | 0.44 | 0.76 | 21 | GOL |
| 3 | 62 | 0.28 | 0.73 | 17 | empty |
Compared structures
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 1XIV · PDBe 1XIV · UniProt Q27743
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