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Glutathione-bound dehydroascorbate reductase 2 of arabidopsis thaliana

Analyse Glutathione-bound dehydroascorbate reductase 2 of arabidopsis thaliana in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5LOL
Type
protein
Length
207 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glutathione S-transferase DHAR2
EC
2.5.1.18
UniProt
Q9FRL8
Ligands
GSH, SO4
Pockets
2 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 11% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlutathione S-transferase DHAR2 (EC 2.5.1.18)protein20755% helix, 11% strandQ9FRL8

Ligands and binding sites

  • GSH · Glutathione · ligand · chains A
  • SO4 · Sulfate ion · ion · chains A
  • GOL · Glycerol · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12510.540.7643GSH
2720.320.7520empty

Compared structures

  • 5LOL · Glutathione-bound Dehydroascorbate Reductase 2 of Arabidopsis thaliana · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9FRL8 · AlphaFold monomer V2.0 prediction for glutathione S-transferase DHAR2 (Q9FRL8) · a predicted model of the same protein · chain A against A, TM-score 0.96

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