Research workbench
Crystal structure of rabbit phosphoglucose isomerase complexed with fructose-6-phosphate
Analyse Crystal structure of rabbit phosphoglucose isomerase complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HOX
- Type
- protein
- Length
- 1,110 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoglucose isomerase
- EC
- 5.3.1.9
- UniProt
- Q9N1E2
- Ligands
- F6P
- Pockets
- 9 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Phosphoglucose isomerase (EC 5.3.1.9) | protein | 555 | 55% helix, 13% strand | Q9N1E2 |
Ligands and binding sites
- F6P · 6-O-phosphono-beta-D-fructofuranose · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 875 | 0.75 | 0.79 | 57 | empty |
| 2 | 334 | 0.70 | 0.83 | 49 | F6P |
| 3 | 359 | 0.70 | 0.83 | 51 | F6P |
| 4 | 65 | 0.42 | 0.81 | 14 | empty |
| 5 | 50 | 0.40 | 0.82 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 6642 Ų buried · 100 hydrogen bonds · protein-protein
Compared structures
- 1HOX · Crystal structure of rabbit phosphoglucose isomerase complexed with fructose-6-phosphate · the same entry in another collection · chain A against A, TM-score 1.00
- Q9N1E2 · AlphaFold monomer V2.0 prediction for glucose-6-phosphate isomerase (Q9N1E2) · a predicted model of the same protein · 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 Q9N1E2
- Elsewhere: RCSB PDB 1HOX · PDBe 1HOX · UniProt Q9N1E2
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