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The 1.35 structure of a viral RNase L antagonist reveals basis for the 2'-5'-oligoadenylate binding and enzyme activity.

Analyse The 1.35 structure of a viral RNase L antagonist reveals basis for the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4YE2
Type
protein
Length
283 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Capping enzyme protein
UniProt
B3F2X4
Ligands
A2P, SO4
Pockets
5 · best druggability 0.53

Structure

x-ray diffraction · 2 distinct chains · 23% helix, 39% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACapping enzyme proteinprotein14223% helix, 40% strandB3F2X4
BCapping enzyme proteinprotein14123% helix, 37% strandB3F2X4

Ligands and binding sites

  • A2P · Adenosine-2'-5'-diphosphate · ligand · chains A
  • SO4 · Sulfate ion · ion · chains 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12390.530.7633A2P
21090.390.7516empty
3820.340.7413empty
4620.300.7523empty
5510.260.7311empty

Interfaces

1 interface between chains.

  • A–B · 490 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 4YE2 · The 1.35 structure of a viral RNase L antagonist reveals basis for the… · the same entry in another collection · chain A against A, TM-score 1.00

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