Research workbench
Crystal structure of the regulatory subunit of aspartate kinase from thermus flavus
Analyse Crystal structure of the regulatory subunit of aspartate kinase from thermus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2DT9
- Type
- protein
- Length
- 306 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartokinase
- EC
- 2.7.2.4
- UniProt
- P61489
- Ligands
- THR
- Pockets
- 4 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Aspartokinase (EC 2.7.2.4) | protein | 153 | 39% helix, 35% strand | P61489 |
Ligands and binding sites
- THR · Threonine · ligand · 2 copies · chains A, B
- ACT · Acetate ion · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.48 | 0.81 | 21 | ACT |
| 2 | 66 | 0.38 | 0.79 | 17 | empty |
| 3 | 79 | 0.37 | 0.77 | 21 | empty |
| 4 | 68 | 0.36 | 0.78 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1954 Ų buried · 27 hydrogen bonds · protein-protein
Compared structures
- 2DT9 · Crystal structure of the regulatory subunit of aspartate kinase from Thermus flavus · the same entry in another collection · chain A against A, TM-score 1.00
- P61489 · AlphaFold monomer V2.0 prediction for aspartokinase (P61489) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P61489
- Elsewhere: RCSB PDB 2DT9 · PDBe 2DT9 · UniProt P61489
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.