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Crystal structure of phosphofructokinase apoenzyme from trypanosoma brucei.
Analyse Crystal structure of phosphofructokinase apoenzyme from trypanosoma brucei. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HIG
- Type
- protein
- Length
- 862 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 6-phospho-1-fructokinase
- EC
- 2.7.1.11
- UniProt
- O15648
- Ligands
- NA
- Pockets
- 15 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 6-phospho-1-fructokinase (EC 2.7.1.11) | protein | 440 | 37% helix, 21% strand | O15648 |
| B | 6-phospho-1-fructokinase (EC 2.7.1.11) | protein | 422 | 38% helix, 21% strand | O15648 |
Ligands and binding sites
- NA · Sodium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 759 | 0.84 | 0.87 | 68 | empty |
| 2 | 456 | 0.71 | 0.81 | 49 | empty |
| 3 | 391 | 0.67 | 0.80 | 48 | empty |
| 4 | 221 | 0.61 | 0.81 | 33 | empty |
| 5 | 149 | 0.53 | 0.80 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 2677 Ų buried · 39 hydrogen bonds · protein-protein
Compared structures
- 2HIG · Crystal Structure of Phosphofructokinase apoenzyme from Trypanosoma brucei. · the same entry in another collection · chain A against A, TM-score 1.00
- O15648 · AlphaFold monomer V2.0 prediction for ATP-dependent 6-phosphofructokinase (O15648) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 O15648
- Elsewhere: RCSB PDB 2HIG · PDBe 2HIG · UniProt O15648
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