Research workbench
Crystal structure of plasmodium falciparum glucose-6-phosphate isomerase (PF14_0341) in complex with fructose-6-phosphate
Analyse Crystal structure of plasmodium falciparum glucose-6-phosphate isomerase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PR3
- Type
- protein
- Length
- 1,155 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucose-6-phosphate isomerase
- EC
- 5.3.1.9
- UniProt
- Q8ILA4
- Ligands
- F6P, PO4
- Pockets
- 13 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucose-6-phosphate isomerase (EC 5.3.1.9) | protein | 578 | 53% helix, 11% strand | Q8ILA4 |
| B | Glucose-6-phosphate isomerase (EC 5.3.1.9) | protein | 577 | 53% helix, 11% strand | Q8ILA4 |
Ligands and binding sites
- F6P · 6-O-phosphono-beta-D-fructofuranose · ligand · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1080 | 0.81 | 0.82 | 74 | empty |
| 2 | 319 | 0.71 | 0.84 | 44 | F6P |
| 3 | 320 | 0.70 | 0.84 | 47 | F6P |
| 4 | 397 | 0.59 | 0.76 | 51 | empty |
| 5 | 182 | 0.51 | 0.78 | 31 | empty |
Interfaces
1 interface between chains.
- A–B · 7101 Ų buried · 100 hydrogen bonds · protein-protein
Compared structures
- 3PR3 · Crystal structure of Plasmodium falciparum glucose-6-phosphate isomerase (PF14_0341) in… · 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 Q8ILA4
- Elsewhere: RCSB PDB 3PR3 · PDBe 3PR3 · UniProt Q8ILA4
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