Research workbench
Aspartate semialdehyde dehydrogenase from francisella tularensis
Analyse Aspartate semialdehyde dehydrogenase from francisella tularensis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4WOJ
- Type
- protein
- Length
- 729 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartate semialdehyde dehydrogenase
- UniProt
- Q8G8T7
- Ligands
- NA, SO4
- Pockets
- 4 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartate semialdehyde dehydrogenase | protein | 364 | 40% helix, 22% strand | Q8G8T7 |
| B | Aspartate semialdehyde dehydrogenase | protein | 365 | 40% helix, 22% strand | Q8G8T7 |
Ligands and binding sites
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 | 446 | 0.65 | 0.78 | 55 | empty |
| 2 | 409 | 0.64 | 0.78 | 53 | empty |
| 3 | 99 | 0.34 | 0.73 | 20 | empty |
| 4 | 52 | 0.27 | 0.74 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 3469 Ų buried · 41 hydrogen bonds · protein-protein
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 Q8G8T7
- Elsewhere: RCSB PDB 4WOJ · PDBe 4WOJ · UniProt Q8G8T7
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