Research workbench
Glucosamine kinase (crystal form a)
Analyse Glucosamine kinase (crystal form a) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HWJ
- Type
- protein
- Length
- 833 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucosamine kinase
- UniProt
- A0A1H7TQR5
- Ligands
- MG, CL
- Pockets
- 7 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucosamine kinase | protein | 428 | 49% helix, 19% strand | A0A1H7TQR5 |
| B | Glucosamine kinase | protein | 405 | 52% helix, 19% strand | A0A1H7TQR5 |
Ligands and binding sites
- MG · Magnesium ion · metal · 7 copies · chains A, B
- CL · Chloride ion · ion · 4 copies · chains A, B
- PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains A
- BTB · 2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1038 | 0.79 | 0.81 | 83 | empty |
| 2 | 466 | 0.73 | 0.82 | 41 | empty |
| 3 | 491 | 0.73 | 0.82 | 45 | BTB |
| 4 | 476 | 0.70 | 0.80 | 51 | PEG |
| 5 | 372 | 0.66 | 0.80 | 55 | MG |
Interfaces
1 interface between chains.
- A–B · 384 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 6HWJ · Glucosamine kinase (crystal form A) · 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 A0A1H7TQR5
- Elsewhere: RCSB PDB 6HWJ · PDBe 6HWJ · UniProt A0A1H7TQR5
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