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Crystal structure of the C. themophilum scavenger decapping enzyme dcps apo form

Analyse Crystal structure of the C. themophilum scavenger decapping enzyme dcps apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6GBS
Type
protein
Length
663 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative mRNA decapping protein
UniProt
G0S8A3
Pockets
8 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APutative mRNA decapping proteinprotein33035% helix, 28% strandG0S8A3
BPutative mRNA decapping proteinprotein33335% helix, 28% strandG0S8A3

Ligands and binding sites

  • EDO · 1,2-ethanediol · additive · 12 copies · chains A, B
  • PEG · Di(hydroxyethyl)ether · additive · chains A, B

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

Pockets

8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12420.820.9551empty
27920.710.7787EDO
32570.520.7526EDO
41780.470.7520empty
5870.440.7925EDO

Interfaces

1 interface between chains.

  • A–B · 4851 Ų buried · 107 hydrogen bonds · protein-protein

Compared structures

  • 6GBS · Crystal Structure of the C. themophilum Scavenger Decapping Enzyme DcpS apo form · the same entry in another collection · chain A against A, TM-score 1.00

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