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Crystal structure of rice dwarf virus P5 in complex with S- adenosylmethionine

Analyse Crystal structure of rice dwarf virus P5 in complex with S- adenosylmethionine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5X6Y
Type
protein
Length
2,960 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
Ligands
SAM
Pockets
20 · best druggability 0.79

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
AMRNA capping enzyme P5 (EC 2.7.7.50)protein77941% helix, 19% strand—
BMRNA capping enzyme P5 (EC 2.7.7.50)protein69440% helix, 18% strand—
CMRNA capping enzyme P5 (EC 2.7.7.50)protein77441% helix, 18% strand—
DMRNA capping enzyme P5 (EC 2.7.7.50)protein71341% helix, 19% strand—

Ligands and binding sites

  • SAM · S-adenosylmethionine · ligand · 5 copies · chains A, B, C
  • EDO · 1,2-ethanediol · additive · 9 copies · chains A, B, C, D
  • FLC · Citrate anion · additive · 3 copies · chains A, B, D

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
11160.790.9840empty
28520.780.8144empty
38700.770.8041empty
4960.770.9819empty
5900.770.9821empty

Interfaces

3 interfaces between chains.

  • A–B · 2944 Ų buried · 47 hydrogen bonds · protein-protein
  • C–D · 2660 Ų buried · 36 hydrogen bonds · protein-protein
  • A–C · 107 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 5X6Y · Crystal structure of Rice Dwarf Virus P5 in complex with S-adenosylmethionine · the same entry in another collection · chain B against B, TM-score 1.00

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