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Crystal structure of the capping enzyme P5 from rice dwarf virus

Analyse Crystal structure of the capping enzyme P5 from rice dwarf virus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5X6X
Type
protein
Length
3,111 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
MRNA capping enzyme P5
EC
2.7.7.50
Pockets
20 · best druggability 0.78

Structure

x-ray diffraction · 4 distinct chains · 41% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
CMRNA capping enzyme P5 (EC 2.7.7.50)protein77940% helix, 19% strand—
AMRNA capping enzyme P5 (EC 2.7.7.50)protein77640% helix, 19% strand—
BMRNA capping enzyme P5 (EC 2.7.7.50)protein77842% helix, 19% strand—
DMRNA capping enzyme P5 (EC 2.7.7.50)protein77841% helix, 19% strand—

Ligands and binding sites

  • EDO · 1,2-ethanediol · additive · 6 copies · chains C, D, A

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11010.780.9822empty
28100.780.8243empty
38730.780.8195empty
4920.780.9922empty
57770.770.8244empty

Interfaces

5 interfaces between chains.

  • C–D · 2990 Ų buried · 49 hydrogen bonds · protein-protein
  • A–B · 2940 Ų buried · 48 hydrogen bonds · protein-protein
  • C–A · 573 Ų buried · 1 hydrogen bond · protein-protein
  • C–B · 348 Ų buried · 9 hydrogen bonds · protein-protein
  • B–D · 155 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 5X6X · Crystal structure of the capping enzyme P5 from Rice Dwarf Virus · the same entry in another collection · chain A against A, TM-score 1.00

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