GL1X · GenesisL1 explorer

Research workbench

Structural basis of salicylic acid perception by arabidopsis npr proteins

Analyse Structural basis of salicylic acid perception by arabidopsis npr proteins in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6WPG
Type
protein
Length
225 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Regulatory protein NPR4
UniProt
Q5ICL9
Ligands
SAL
Pockets
3 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 75% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARegulatory protein NPR4protein11970% helix, 0% strandQ5ICL9
BRegulatory protein NPR4protein10680% helix, 0% strandQ5ICL9

Ligands and binding sites

  • SAL · 2-hydroxybenzoic acid · ligand · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1550.720.9916SAL
2540.720.9916SAL
3700.340.7512empty

Interfaces

1 interface between chains.

  • A–B · 965 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 6WPG · Structural Basis of Salicylic Acid Perception by Arabidopsis NPR Proteins · the same entry in another collection · chain A against A, TM-score 1.00
  • Q5ICL9 · AlphaFold monomer V2.0 prediction for regulatory protein NPR4 (Q5ICL9) · a predicted model of the same protein · chain B against A, TM-score 0.84

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.