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Crystal structure of the tir domain from the arabidopsis thaliana disease resistance protein RPS4

Analyse Crystal structure of the tir domain from the arabidopsis thaliana disease… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4C6R
Type
protein
Length
648 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Disease resistance protein RPS4
UniProt
Q9XGM3
Pockets
4 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DDisease resistance protein RPS4protein16255% helix, 14% strandQ9XGM3

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12970.650.8134empty
2500.470.8514empty
31340.450.7720empty
4650.290.7415empty

Interfaces

3 interfaces between chains.

  • C–D · 350 Ų buried · 2 hydrogen bonds · protein-protein
  • B–D · 288 Ų buried · 4 hydrogen bonds · protein-protein
  • A–C · 11 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 4C6R · Crystal structure of the TIR domain from the Arabidopsis Thaliana disease resistance… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9XGM3 · AlphaFold monomer V2.0 prediction for disease resistance protein RPS4 (Q9XGM3) · a predicted model of the same protein · chain A against A, TM-score 0.93

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