Research workbench
Structure of glucose 6-phosphate isomerase from staphylococcus aureus
Analyse Structure of glucose 6-phosphate isomerase from staphylococcus aureus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FF1
- Type
- protein
- Length
- 888 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
- Q5HHC2
- Ligands
- G6Q, NA
- Pockets
- 9 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glucose-6-phosphate isomerase (EC 5.3.1.9) | protein | 444 | 55% helix, 13% strand | Q5HHC2 |
Ligands and binding sites
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 | 1108 | 0.76 | 0.78 | 87 | empty |
| 2 | 326 | 0.59 | 0.77 | 38 | empty |
| 3 | 306 | 0.58 | 0.77 | 31 | empty |
| 4 | 113 | 0.44 | 0.78 | 29 | NA |
| 5 | 110 | 0.42 | 0.77 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 904 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 modified (engineered).
Compared structures
- 3FF1 · Structure of Glucose 6-phosphate Isomerase from Staphylococcus aureus · the same entry in another collection · chain A against A, TM-score 1.00
- Q5HHC2 · AlphaFold monomer V2.0 prediction for glucose-6-phosphate isomerase (Q5HHC2) · 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 Q5HHC2
- Elsewhere: RCSB PDB 3FF1 · PDBe 3FF1 · UniProt Q5HHC2
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