Research workbench
Glucose-6-phosphate dehydrogenase in complex with its substrate glucose-6-phosphate
Analyse Glucose-6-phosphate dehydrogenase in complex with its substrate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7E6I
- Type
- protein
- Length
- 484 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucose-6-phosphate 1-dehydrogenase
- EC
- 1.1.1.49
- UniProt
- P48828
- Ligands
- BG6
- Pockets
- 5 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucose-6-phosphate 1-dehydrogenase (EC 1.1.1.49) | protein | 484 | 36% helix, 21% strand | P48828 |
Ligands and binding sites
- BG6 · 6-O-phosphono-beta-D-glucopyranose · sugar · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
- 7PE · 2-(2-(2-(2-(2-(2-ethoxyethoxy)ethoxy)ethoxy)ethoxy) ethoxy)ethanol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 281 | 0.59 | 0.78 | 42 | BG6 |
| 2 | 217 | 0.49 | 0.75 | 29 | empty |
| 3 | 75 | 0.46 | 0.82 | 20 | empty |
| 4 | 137 | 0.44 | 0.76 | 26 | empty |
| 5 | 103 | 0.39 | 0.76 | 21 | empty |
Compared structures
- 7E6I · Glucose-6-phosphate dehydrogenase in complex with its substrate glucose-6-phosphate · the same entry in another collection · chain A against A, TM-score 1.00
- P48828 · AlphaFold monomer V2.0 prediction for glucose-6-phosphate 1-dehydrogenase (P48828) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P48828
- Elsewhere: RCSB PDB 7E6I · PDBe 7E6I · UniProt P48828
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