Research workbench
Crystal structure of fbp aldolase from toxoplasma gondii, schiff base fbp complex
Analyse Crystal structure of fbp aldolase from toxoplasma gondii, schiff base fbp… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5TKN
- Type
- protein
- Length
- 349 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose-bisphosphate aldolase
- EC
- 4.1.2.13
- UniProt
- Q8I8I2
- Ligands
- P6F
- Pockets
- 2 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructose-bisphosphate aldolase (EC 4.1.2.13) | protein | 349 | 47% helix, 15% strand | Q8I8I2 |
Ligands and binding sites
- P6F · 1,6-di-O-phosphono-D-fructose · ligand · chains A
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 | 181 | 0.63 | 0.84 | 25 | P6F |
| 2 | 107 | 0.49 | 0.81 | 25 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
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 Q8I8I2
- Elsewhere: RCSB PDB 5TKN · PDBe 5TKN · UniProt Q8I8I2
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