Research workbench
Kinetic and structural characterization of plasmodium falciparum glutamate dehydrogenase 2
Analyse Kinetic and structural characterization of plasmodium falciparum glutamate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3R3J
- Type
- protein
- Length
- 2,736 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate dehydrogenase
- EC
- 1.4.1.3
- UniProt
- Q8ILF7
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Glutamate dehydrogenase (EC 1.4.1.3) | protein | 456 | 50% helix, 15% strand | Q8ILF7 |
Pockets
20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 275 | 0.85 | 0.96 | 32 | empty |
| 2 | 270 | 0.84 | 0.95 | 33 | empty |
| 3 | 290 | 0.84 | 0.94 | 31 | empty |
| 4 | 917 | 0.82 | 0.84 | 141 | empty |
| 5 | 623 | 0.81 | 0.86 | 100 | empty |
Interfaces
12 interfaces between chains.
- A–E · 1708 Ų buried · 31 hydrogen bonds · protein-protein
- B–C · 1704 Ų buried · 29 hydrogen bonds · protein-protein
- D–F · 1683 Ų buried · 31 hydrogen bonds · protein-protein
- C–F · 1191 Ų buried · 15 hydrogen bonds · protein-protein
- B–D · 1154 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 3R3J · Kinetic and structural characterization of Plasmodium falciparum glutamate dehydrogenase 2 · 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 Q8ILF7
- Elsewhere: RCSB PDB 3R3J · PDBe 3R3J · UniProt Q8ILF7
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