Research workbench
Glucose 6-phosphate dehydrogenase from leuconostoc mesenteroides
Analyse Glucose 6-phosphate dehydrogenase from leuconostoc mesenteroides in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DPG
- Type
- protein
- Length
- 970 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucose 6-phosphate dehydrogenase
- EC
- 1.1.1.49
- UniProt
- P11411
- Ligands
- PO4
- Pockets
- 10 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glucose 6-phosphate dehydrogenase (EC 1.1.1.49) | protein | 485 | 40% helix, 20% strand | P11411 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 416 | 0.65 | 0.78 | 52 | PO4 |
| 2 | 355 | 0.59 | 0.76 | 45 | PO4 |
| 3 | 131 | 0.50 | 0.79 | 23 | empty |
| 4 | 83 | 0.46 | 0.81 | 19 | empty |
| 5 | 101 | 0.45 | 0.79 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 2347 Ų buried · 27 hydrogen bonds · protein-protein
Compared structures
- 1DPG · Glucose 6-phosphate dehydrogenase from leuconostoc mesenteroides · the same entry in another collection · chain A against A, TM-score 1.00
- P11411 · AlphaFold monomer V2.0 prediction for glucose-6-phosphate 1-dehydrogenase (P11411) · 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 P11411
- Elsewhere: RCSB PDB 1DPG · PDBe 1DPG · UniProt P11411
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