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Crystal structure of saccharomyces cerevisiae DCP2 nudix domain (E198Q mutation)

Analyse Crystal structure of saccharomyces cerevisiae DCP2 nudix domain (E198Q mutation) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4KG4
Type
protein
Length
279 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
MRNA-decapping enzyme subunit 2
EC
3.-.-.-
UniProt
P53550
Pockets
4 · best druggability 0.52

Structure

x-ray diffraction · 2 distinct chains · 25% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMRNA-decapping enzyme subunit 2 (EC 3.-.-.-)protein13827% helix, 31% strandP53550
BMRNA-decapping enzyme subunit 2 (EC 3.-.-.-)protein14123% helix, 35% strandP53550

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12980.520.7542empty
2740.350.7719empty
3880.340.7417empty
4500.290.7511empty

Interfaces

1 interface between chains.

  • A–B · 532 Ų buried · 9 hydrogen bonds · protein-protein

Compared structures

  • 4KG4 · Crystal structure of Saccharomyces cerevisiae Dcp2 Nudix domain (E198Q mutation) · the same entry in another collection · chain A against A, TM-score 1.00
  • P53550 · AlphaFold monomer V2.0 prediction for M7GPPPN-mRNA hydrolase (P53550) · a predicted model of the same protein · chain A against A, TM-score 0.97

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