Research workbench
The crystal structure of phosphoglucose isomerase from pyrococcus furiosus in complex with sorbitol 6-phosphate and zinc
Analyse The crystal structure of phosphoglucose isomerase from pyrococcus furiosus in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GC1
- Type
- protein
- Length
- 376 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
- P83194
- Ligands
- S6P, ZN
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glucose-6-phosphate isomerase (EC 5.3.1.9) | protein | 188 | 11% helix, 46% strand | P83194 |
Ligands and binding sites
- S6P · D-sorbitol-6-phosphate · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 210 | 0.68 | 0.86 | 34 | S6P |
| 2 | 156 | 0.66 | 0.87 | 28 | S6P |
Interfaces
1 interface between chains.
- A–B · 1967 Ų buried · 31 hydrogen bonds · protein-protein
Compared structures
- 2GC1 · The crystal structure of phosphoglucose isomerase from Pyrococcus furiosus in complex… · the same entry in another collection · chain A against A, TM-score 1.00
- P83194 · AlphaFold monomer V2.0 prediction for glucose-6-phosphate isomerase (P83194) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 P83194
- Elsewhere: RCSB PDB 2GC1 · PDBe 2GC1 · UniProt P83194
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