Research workbench
Drosophila obp lush D118A mutation
Analyse Drosophila obp lush D118A mutation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QDI
- Type
- protein
- Length
- 248 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- General odorant-binding protein lush
- UniProt
- O02372
- Pockets
- 3 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 67% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | General odorant-binding protein lush | protein | 124 | 67% helix, 2% strand | O02372 |
Ligands and binding sites
- PGE · Triethylene glycol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 211 | 0.80 | 0.93 | 32 | PGE |
| 2 | 213 | 0.78 | 0.91 | 32 | PGE |
| 3 | 250 | 0.63 | 0.81 | 41 | empty |
Interfaces
1 interface between chains.
- A–B · 605 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
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 O02372
- Elsewhere: RCSB PDB 2QDI · PDBe 2QDI · UniProt O02372
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