Research workbench
Crystal structure of rabbit phosphoglucose isomerase complexed with sorbitol-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
- 1XTB
- Type
- protein
- Length
- 1,112 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
- S6P
- Pockets
- 8 · best druggability 0.77
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 | 556 | 55% helix, 13% strand | Q9N1E2 |
Ligands and binding sites
- S6P · D-sorbitol-6-phosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1121 | 0.77 | 0.79 | 63 | empty |
| 2 | 362 | 0.70 | 0.83 | 52 | S6P |
| 3 | 296 | 0.69 | 0.83 | 37 | S6P |
| 4 | 95 | 0.41 | 0.77 | 15 | empty |
| 5 | 119 | 0.38 | 0.74 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 6766 Ų buried · 94 hydrogen bonds · protein-protein
Compared structures
- 1XTB · Crystal Structure of Rabbit Phosphoglucose Isomerase Complexed with Sorbitol-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 B 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 1XTB · PDBe 1XTB · UniProt Q9N1E2
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