Research workbench
Structure of oye from geobacillus kaustophilus, orthorhombic crystal form
Analyse Structure of oye from geobacillus kaustophilus, orthorhombic crystal form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3GR8
- Type
- protein
- Length
- 680 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NADPH dehydrogenase
- EC
- 1.6.99.1
- UniProt
- Q5KXG9
- Ligands
- FMN, SO4
- Pockets
- 4 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | NADPH dehydrogenase (EC 1.6.99.1) | protein | 340 | 37% helix, 16% strand | Q5KXG9 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · chains A, B
- BTB · 2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 233 | 0.56 | 0.78 | 37 | FMN |
| 2 | 215 | 0.55 | 0.79 | 41 | empty |
| 3 | 243 | 0.55 | 0.77 | 37 | FMN |
| 4 | 189 | 0.43 | 0.73 | 27 | BTB |
Interfaces
1 interface between chains.
- A–B · 533 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 3GR8 · Structure of OYE from Geobacillus kaustophilus, orthorhombic crystal form · the same entry in another collection · chain A against A, TM-score 1.00
- Q5KXG9 · AlphaFold monomer V2.0 prediction for NADPH dehydrogenase (Q5KXG9) · 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 Q5KXG9
- Elsewhere: RCSB PDB 3GR8 · PDBe 3GR8 · UniProt Q5KXG9
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