Research workbench
Reduced precursor form of glucose-fructose oxidoreductase from zymomonas mobilis complexed with glycerol
Analyse Reduced precursor form of glucose-fructose oxidoreductase from zymomonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1H6B
- Type
- protein
- Length
- 762 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Precursor form of glucose-fructose oxidoreductase
- EC
- 1.1.99.28
- UniProt
- P75002
- Ligands
- NDP
- Pockets
- 8 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Precursor form of glucose-fructose oxidoreductase (EC 1.1.99.28) | protein | 381 | 37% helix, 23% strand | P75002 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- GOL · Glycerol · additive · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1066 | 0.81 | 0.82 | 117 | NDP, GOL |
| 2 | 83 | 0.63 | 0.90 | 23 | empty |
| 3 | 110 | 0.44 | 0.78 | 21 | empty |
| 4 | 129 | 0.43 | 0.76 | 25 | empty |
| 5 | 84 | 0.37 | 0.76 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1697 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
- 1H6B · Reduced Precursor Form of Glucose-Fructose Oxidoreductase from Zymomonas mobilis… · the same entry in another collection · 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 P75002
- Elsewhere: RCSB PDB 1H6B · PDBe 1H6B · UniProt P75002
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