MolNFT v1 · #32554 · protein
Acetylglutamate kinase from thermotoga maritima complexed with its inhibitor arginine
2BTY: “Acetylglutamate kinase from thermotoga maritima complexed with its inhibitor arginine”. X-ray diffraction, 3 ligands (ARG, NLG, K), 12 pockets (best druggability 0.63). MolNFT v1 #32554 on GenesisL1: 3D structure, binding sites and…
- PDB
- 2BTY
- Type
- protein
- Length
- 846 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylglutamate kinase
- EC
- 2.7.2.8
- UniProt
- Q9X2A4
- Ligands
- ARG, NLG, K
- Pockets
- 12 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Acetylglutamate kinase (EC 2.7.2.8) | protein | 282 | 43% helix, 23% strand | Q9X2A4 |
Ligands and binding sites
- ARG · Arginine · ligand · 3 copies · chains A, B, C
- NLG · N-acetyl-L-glutamate · ligand · 3 copies · chains A, B, C
- K · Potassium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 484 | 0.63 | 0.76 | 79 | NLG |
| 2 | 317 | 0.55 | 0.75 | 37 | NLG |
| 3 | 266 | 0.50 | 0.74 | 39 | NLG |
| 4 | 163 | 0.47 | 0.76 | 28 | empty |
| 5 | 109 | 0.45 | 0.79 | 29 | K |
Interfaces
2 interfaces between chains.
- A–B · 1385 Ų buried · 17 hydrogen bonds · protein-protein
- A–C · 1219 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 2BTY · Acetylglutamate kinase from Thermotoga maritima complexed with its inhibitor arginine · the same entry in another collection · chain B against B, TM-score 1.00
- Q9X2A4 · AlphaFold monomer V2.0 prediction for acetylglutamate kinase (Q9X2A4) · 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 Q9X2A4
- Elsewhere: RCSB PDB 2BTY · PDBe 2BTY · UniProt Q9X2A4
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.