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Crystal structure of lush from drosophila melanogaster: apo protein

Analyse Crystal structure of lush from drosophila melanogaster: apo protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1T14
Type
protein
Length
248 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Lush
UniProt
O02372
Pockets
5 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 65% helix, 2% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BLushprotein12465% helix, 2% strandO02372

Ligands and binding sites

  • ACT · Acetate ion · 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12060.810.9428ACT
21960.790.9331ACT
31750.540.8033empty
4610.350.7711empty
5680.350.7611empty

Interfaces

1 interface between chains.

  • A–B · 714 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 1T14 · Crystal structure of LUSH from Drosophila melanogaster: apo protein · 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

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