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Structure of the activated ROQ1 resistosome directly recognizing the pathogen effector xopq

Analyse Structure of the activated ROQ1 resistosome directly recognizing the pathogen… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7JLV
Type
protein
Length
1,748 residues
Chains
4
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Disease resistance protein ROQ1
EC
3.2.2.6
UniProt
A0A290U7C4
Ligands
ATP, MG
Pockets
20 · best druggability 0.81

Structure

electron microscopy · 1 distinct chain · 42% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, D, GDisease resistance protein ROQ1 (EC 3.2.2.6)protein43742% helix, 10% strandA0A290U7C4

Ligands and binding sites

  • ATP · Adenosine-5'-triphosphate · ligand · 4 copies · chains A, B, D, G
  • MG · Magnesium ion · metal · 4 copies · chains A, B, D, G

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

Pockets

20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19940.810.82100ATP, MG
24360.740.8463ATP, MG
33450.730.8545empty
42820.710.8539empty
52280.690.8628empty

Interfaces

4 interfaces between chains.

  • A–B · 1166 Ų buried · 10 hydrogen bonds · protein-protein
  • D–G · 1165 Ų buried · 10 hydrogen bonds · protein-protein
  • B–D · 1163 Ų buried · 10 hydrogen bonds · protein-protein
  • A–G · 1158 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 7JLV · Structure of the activated Roq1 resistosome directly recognizing the pathogen effector… · the same entry in another collection · chain A against A, TM-score 1.00

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