MolNFT v1 · #39250 · protein
Crystal structure of N-acetylglucosamine kinase (TM1224) from thermotoga maritima at 2.46 a resolution
2HOE: “Crystal structure of N-acetylglucosamine kinase (TM1224) from thermotoga maritima at 2.46 a resolution”. X-ray diffraction, 1 ligand (K), 2 pockets (best druggability 0.60). MolNFT v1 #39250 on GenesisL1: 3D structure, binding sites…
- PDB
- 2HOE
- Type
- protein
- Length
- 354 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-acetylglucosamine kinase
- EC
- 2.7.1.59
- UniProt
- Q9X0V1
- Ligands
- K
- Pockets
- 2 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetylglucosamine kinase (EC 2.7.1.59) | protein | 354 | 45% helix, 23% strand | Q9X0V1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 274 | 0.60 | 0.79 | 42 | GOL |
| 2 | 162 | 0.48 | 0.77 | 26 | empty |
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 2HOE · Crystal structure of N-acetylglucosamine kinase (TM1224) from Thermotoga maritima at 2.46… · the same entry in another collection · chain A against A, 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 Q9X0V1
- Elsewhere: RCSB PDB 2HOE · PDBe 2HOE · UniProt Q9X0V1
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.