MolNFT v1 · #105017 · protein
Arabidopsis hexokinase 1 (ATHXK1) structure in glucose-bound form
4QS7 · Hexokinase-1: “Arabidopsis hexokinase 1 (ATHXK1) structure in glucose-bound form”. X-ray diffraction, 1 ligand (BGC), 1 pocket (best druggability 0.71). MolNFT v1 #105017 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4QS7
- Type
- protein
- Length
- 455 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hexokinase-1
- EC
- 2.7.1.1
- UniProt
- Q42525
- Ligands
- BGC
- Pockets
- 1 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hexokinase-1 (EC 2.7.1.1) | protein | 455 | 47% helix, 18% strand | Q42525 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 525 | 0.71 | 0.80 | 61 | BGC |
Compared structures
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 Q42525
- Elsewhere: RCSB PDB 4QS7 · PDBe 4QS7 · UniProt Q42525
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