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Getah virus macro domain in complex with adpr covalently bond to CYS34

Analyse Getah virus macro domain in complex with adpr covalently bond to CYS34 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6R0R
Type
protein
Length
162 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Non-structural polyprotein
UniProt
A0A143SL92
Ligands
JNT
Pockets
1 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANon-structural polyproteinprotein16236% helix, 21% strandA0A143SL92

Ligands and binding sites

  • JNT · [[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2~{R},3~{S},4~{S})-2,3,4,5-tetrakis(oxidanyl)pentyl] hydrogen phosphate · ligand · chains A
  • EDO · 1,2-ethanediol · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11840.590.8228JNT

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

  • 6R0R · Getah virus macro domain in complex with ADPr covalently bond to Cys34 · the same entry in another collection · chain A against A, TM-score 1.00

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