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Crystal structure of drosophila melanogaster translin protein

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

PDB
2QVA
Type
protein
Length
731 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
GM27569P
UniProt
Q7JVK6
Pockets
6 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 79% helix, 1% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, DGM27569Pprotein18280% helix, 1% strandQ7JVK6
CGM27569Pprotein18578% helix, 2% strandQ7JVK6

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13590.590.7636empty
22800.510.7436empty
3550.350.7920empty
4910.340.7418empty
5700.300.7311empty

Interfaces

3 interfaces between chains.

  • B–C · 1782 Ų buried · 16 hydrogen bonds · protein-protein
  • A–D · 550 Ų buried · 2 hydrogen bonds · protein-protein
  • A–C · 292 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 2QVA · Crystal structure of Drosophila melanogaster Translin protein · the same entry in another collection · chain A against A, TM-score 1.00

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