Research workbench
Crystal structure of D38C glucose dehydrogenase mutant from haloferax mediterranei
Analyse Crystal structure of D38C glucose dehydrogenase mutant from haloferax… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2B5W
- Type
- protein
- Length
- 357 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucose dehydrogenase
- EC
- 1.1.1.47
- UniProt
- Q977U7
- Ligands
- NAP, K, ZN
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucose dehydrogenase (EC 1.1.1.47) | protein | 357 | 32% helix, 27% strand | Q977U7 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- K · Potassium ion · metal · 5 copies · chains A
- ZN · Zinc ion · metal · chains A
- FLC · Citrate anion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 583 | 0.70 | 0.79 | 53 | K, NAP |
| 2 | 174 | 0.45 | 0.75 | 25 | empty |
| 3 | 75 | 0.34 | 0.75 | 15 | K |
Compared structures
- 2B5W · Crystal structure of D38C glucose dehydrogenase mutant from Haloferax mediterranei · the same entry in another collection · chain A against A, TM-score 1.00
- Q977U7 · AlphaFold monomer V2.0 prediction for glucose 1-dehydrogenase (Q977U7) · 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 Q977U7
- Elsewhere: RCSB PDB 2B5W · PDBe 2B5W · UniProt Q977U7
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