Research workbench
Crystal structure of fructose-1-phosphate kinase from bacillus halodurans
Analyse Crystal structure of fructose-1-phosphate kinase from bacillus halodurans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ABQ
- Type
- protein
- Length
- 612 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose 1-phosphate kinase
- UniProt
- Q9KEM5
- Ligands
- PO4
- Pockets
- 3 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Fructose 1-phosphate kinase | protein | 306 | 40% helix, 25% strand | Q9KEM5 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 604 | 0.66 | 0.76 | 64 | PO4 |
| 2 | 551 | 0.65 | 0.76 | 64 | PO4 |
| 3 | 55 | 0.31 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1215 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 2ABQ · Crystal structure of fructose-1-phosphate kinase from Bacillus halodurans · 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 Q9KEM5
- Elsewhere: RCSB PDB 2ABQ · PDBe 2ABQ · UniProt Q9KEM5
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