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Asymmetric trimer of the drosophila melanogaster DCP1 C- terminal domain

Analyse Asymmetric trimer of the drosophila melanogaster DCP1 C- terminal domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2WX4
Type
protein
Length
255 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Decapping protein 1
UniProt
Q9W1H5
Ligands
SO4
Pockets
2 · best druggability 0.63

Structure

x-ray diffraction · 6 distinct chains · 79% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ADecapping protein 1protein3871% helix, 0% strandQ9W1H5
BDecapping protein 1protein4180% helix, 0% strandQ9W1H5
CDecapping protein 1protein4381% helix, 0% strandQ9W1H5
DDecapping protein 1protein4573% helix, 0% strandQ9W1H5
EDecapping protein 1protein4386% helix, 0% strandQ9W1H5
FDecapping protein 1protein4582% helix, 0% strandQ9W1H5

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 5 copies · chains A, D, E, C, F

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14170.630.7744SO4
2880.370.7615empty

Interfaces

10 interfaces between chains.

  • A–B · 1027 Ų buried · 2 hydrogen bonds · protein-protein
  • D–E · 957 Ų buried · 4 hydrogen bonds · protein-protein
  • E–F · 911 Ų buried · 7 hydrogen bonds · protein-protein
  • B–C · 822 Ų buried · 5 hydrogen bonds · protein-protein
  • A–C · 793 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 2WX4 · Asymmetric trimer of the Drosophila melanogaster DCP1 C-terminal domain · the same entry in another collection · chain A against A, TM-score 1.00

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