Research workbench
Crystal structure of fructokinase from vibrio cholerae O395 in fructose bound form
Analyse Crystal structure of fructokinase from vibrio cholerae O395 in fructose bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5F11
- Type
- protein
- Length
- 308 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructokinase
- EC
- 2.7.1.4
- UniProt
- A0A0H3AER7
- Ligands
- FRU, NA
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructokinase (EC 2.7.1.4) | protein | 308 | 42% helix, 23% strand | A0A0H3AER7 |
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 | 470 | 0.70 | 0.81 | 58 | FRU |
| 2 | 100 | 0.42 | 0.78 | 14 | empty |
Compared structures
- 5F11 · Crystal structure of Fructokinase from Vibrio cholerae O395 in fructose bound form · 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 A0A0H3AER7
- Elsewhere: RCSB PDB 5F11 · PDBe 5F11 · UniProt A0A0H3AER7
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