MolNFT v1 · #17284 · protein
Complex of drosophila odorant binding protein lush with ethanol
1OOF: “Complex of drosophila odorant binding protein lush with ethanol”. X-ray diffraction, 5 pockets (best druggability 0.80). MolNFT v1 #17284 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1OOF
- Type
- protein
- Length
- 248 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Odorant binding protein lush
- UniProt
- O02372
- Pockets
- 5 · 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 | Odorant binding protein lush | protein | 124 | 67% helix, 2% strand | O02372 |
Ligands and binding sites
- ACT · Acetate ion · additive · 4 copies · chains A, B
- EOH · Ethanol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 218 | 0.80 | 0.93 | 31 | ACT, EOH |
| 2 | 213 | 0.79 | 0.92 | 28 | ACT, EOH |
| 3 | 177 | 0.54 | 0.79 | 31 | empty |
| 4 | 81 | 0.43 | 0.79 | 14 | empty |
| 5 | 68 | 0.34 | 0.76 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 699 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 1OOF · Complex of Drosophila odorant binding protein LUSH with ethanol · the same entry in another collection · chain A against A, TM-score 1.00
- O02372 · AlphaFold monomer V2.0 prediction for general odorant-binding protein lush (O02372) · 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 O02372
- Elsewhere: RCSB PDB 1OOF · PDBe 1OOF · UniProt O02372
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