MolNFT v1 · #32570 · protein
Arginine feed-back inhibitable acetylglutamate kinase
2BUF: “Arginine feed-back inhibitable acetylglutamate kinase”. X-ray diffraction, 4 ligands (NLG, ADP, MG), 20 pockets (best druggability 0.83). MolNFT v1 #32570 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2BUF
- Type
- protein
- Length
- 3,483 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylglutamate kinase
- EC
- 2.7.2.8
- UniProt
- Q9HTN2
- Ligands
- NLG, ADP, MG, CL
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 12 distinct chains · 41% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetylglutamate kinase (EC 2.7.2.8) | protein | 292 | 42% helix, 23% strand | Q9HTN2 |
| B | Acetylglutamate kinase (EC 2.7.2.8) | protein | 296 | 43% helix, 22% strand | Q9HTN2 |
| C | Acetylglutamate kinase (EC 2.7.2.8) | protein | 298 | 40% helix, 22% strand | Q9HTN2 |
| D | Acetylglutamate kinase (EC 2.7.2.8) | protein | 294 | 41% helix, 22% strand | Q9HTN2 |
| E | Acetylglutamate kinase (EC 2.7.2.8) | protein | 287 | 42% helix, 21% strand | Q9HTN2 |
| F | Acetylglutamate kinase (EC 2.7.2.8) | protein | 291 | 44% helix, 19% strand | Q9HTN2 |
| G | Acetylglutamate kinase (EC 2.7.2.8) | protein | 297 | 40% helix, 21% strand | Q9HTN2 |
| H | Acetylglutamate kinase (EC 2.7.2.8) | protein | 295 | 40% helix, 21% strand | Q9HTN2 |
| I | Acetylglutamate kinase (EC 2.7.2.8) | protein | 288 | 43% helix, 21% strand | Q9HTN2 |
| J | Acetylglutamate kinase (EC 2.7.2.8) | protein | 279 | 41% helix, 18% strand | Q9HTN2 |
| K | Acetylglutamate kinase (EC 2.7.2.8) | protein | 273 | 42% helix, 18% strand | Q9HTN2 |
| L | Acetylglutamate kinase (EC 2.7.2.8) | protein | 293 | 41% helix, 21% strand | Q9HTN2 |
Ligands and binding sites
- NLG · N-acetyl-L-glutamate · ligand · 10 copies · chains A, B, D, E, F, G, H, I, K, L
- ADP · Adenosine-5'-diphosphate · ligand · 10 copies · chains B, C, I, D, E, F, G, H, J, L
- MG · Magnesium ion · metal · 8 copies · chains B, E, G, H, I, L
- CL · Chloride ion · ion · 6 copies · chains B, C, D, G, H, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1068 | 0.83 | 0.84 | 128 | ADP, MG, NLG |
| 2 | 57 | 0.69 | 0.96 | 17 | empty |
| 3 | 327 | 0.67 | 0.81 | 39 | ADP, MG, NLG |
| 4 | 331 | 0.66 | 0.81 | 38 | ADP, MG, NLG, CL |
| 5 | 494 | 0.66 | 0.78 | 58 | NLG |
Interfaces
14 interfaces between chains.
- G–H · 1480 Ų buried · 19 hydrogen bonds · protein-protein
- E–F · 1468 Ų buried · 20 hydrogen bonds · protein-protein
- I–J · 1459 Ų buried · 18 hydrogen bonds · protein-protein
- B–C · 1427 Ų buried · 2 hydrogen bonds · protein-protein
- G–I · 1424 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 2BUF · Arginine Feed-Back Inhibitable Acetylglutamate Kinase · the same entry in another collection · chain L against L, TM-score 1.00
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 Q9HTN2
- Elsewhere: RCSB PDB 2BUF · PDBe 2BUF · UniProt Q9HTN2
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.