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The crystal structure of plasmodium falciparum glutamate dehydrogenase, a putative target for novel antimalarial drugs
Analyse The crystal structure of plasmodium falciparum glutamate dehydrogenase, a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BMA
- Type
- protein
- Length
- 2,802 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate dehydrogenase (NADP+)
- EC
- 1.4.1.4
- UniProt
- O96940
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Glutamate dehydrogenase (NADP+) (EC 1.4.1.4) | protein | 467 | 49% helix, 15% strand | O96940 |
Pockets
20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 189 | 0.82 | 0.97 | 29 | empty |
| 2 | 185 | 0.82 | 0.96 | 31 | empty |
| 3 | 184 | 0.81 | 0.96 | 31 | empty |
| 4 | 830 | 0.81 | 0.83 | 120 | empty |
| 5 | 1182 | 0.79 | 0.81 | 152 | empty |
Interfaces
12 interfaces between chains.
- A–E · 1679 Ų buried · 43 hydrogen bonds · protein-protein
- B–C · 1677 Ų buried · 41 hydrogen bonds · protein-protein
- D–F · 1668 Ų buried · 43 hydrogen bonds · protein-protein
- A–F · 1080 Ų buried · 21 hydrogen bonds · protein-protein
- B–E · 1079 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
- 2BMA · The crystal structure of Plasmodium falciparum glutamate dehydrogenase, a putative target… · the same entry in another collection · 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 O96940
- Elsewhere: RCSB PDB 2BMA · PDBe 2BMA · UniProt O96940
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