Research workbench
Crystal structure of the E243D mutant of aspartate semialdehyde dehydrogenase from haemophilus influenzae bound with substrate aspartate semialdehyde
Analyse Crystal structure of the E243D mutant of aspartate semialdehyde dehydrogenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Q2X
- Type
- protein
- Length
- 714 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartate-semialdehyde dehydrogenase
- EC
- 1.2.1.11
- UniProt
- P44801
- Pockets
- 6 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Aspartate-semialdehyde dehydrogenase (EC 1.2.1.11) | protein | 357 | 41% helix, 22% strand | P44801 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 336 | 0.59 | 0.77 | 39 | empty |
| 2 | 332 | 0.58 | 0.76 | 39 | empty |
| 3 | 80 | 0.36 | 0.76 | 15 | empty |
| 4 | 64 | 0.31 | 0.75 | 15 | empty |
| 5 | 60 | 0.30 | 0.75 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 3550 Ų buried · 44 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- 1Q2X · Crystal Structure of the E243D Mutant of Aspartate Semialdehyde Dehydrogenase from… · the same entry in another collection · chain A against A, TM-score 1.00
- P44801 · AlphaFold monomer V2.0 prediction for aspartate-semialdehyde dehydrogenase (P44801) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 P44801
- Elsewhere: RCSB PDB 1Q2X · PDBe 1Q2X · UniProt P44801
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