Research workbench
The structure of a probable aspartate-semialdehyde dehydrogenase from pseudomonas aeruginosa
Analyse The structure of a probable aspartate-semialdehyde dehydrogenase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HJS
- Type
- protein
- Length
- 334 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Usg-1 protein homolog
- UniProt
- O87014
- Pockets
- 4 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Usg-1 protein homolog | protein | 334 | 37% helix, 24% strand | O87014 |
Ligands and binding sites
- DIO · 1,4-diethylene dioxide · additive · 10 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 369 | 0.61 | 0.77 | 41 | DIO |
| 2 | 87 | 0.37 | 0.76 | 18 | DIO |
| 3 | 70 | 0.37 | 0.77 | 15 | empty |
| 4 | 58 | 0.28 | 0.74 | 17 | empty |
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 2HJS · The structure of a probable aspartate-semialdehyde dehydrogenase from Pseudomonas… · the same entry in another collection · chain A against A, TM-score 1.00
- O87014 · AlphaFold monomer V2.0 prediction for usg-1 protein homolog (O87014) · a predicted model of the same protein · chain A 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 O87014
- Elsewhere: RCSB PDB 2HJS · PDBe 2HJS · UniProt O87014
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