› 5n9u

Solution NMR

Dehydroascorbate reductase 3A from Populus trichocarpa complexed with GSH.

Released:
DOI: 10.2210/pdb5n9u/pdb
PDB entry 5n9u coloured by chain, ensemble of 10 models, front view.
PDB entry 5n9u coloured by chain, ensemble of 10 models, side view.
PDB entry 5n9u coloured by chain, ensemble of 10 models, top view.
Source organism: Populus trichocarpa
Primary publication:
Insights into ascorbate regeneration in plants: investigating the redox and structural properties of dehydroascorbate reductases from Populus trichocarpa.
Lallement PA, Roret T, Tsan P, Gualberto JM, Girardet JM, Didierjean C, Rouhier N, Hecker A
Biochem J 473 717-31 (2016)
PMID: 26699905

Function and Biology Details

Reaction catalysed: 
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-110825 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dehydroascorbate reductase family protein Chain: A
Molecule details ›
Chain: A
Length: 218 amino acids
Theoretical weight: 24.36 KDa
Source organism: Populus trichocarpa
Expression system: Escherichia coli
UniProt:
  • Canonical: B9HM36 (Residues: 1-212; Coverage: 100%)
Gene name: POPTR_008G049300
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GSH 1 x GSH
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 14%
Refinement method: molecular dynamics
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Recent Developments in Enzymatic Antioxidant Defence Mechanism in Plants with Special Reference to Abiotic Stress.
Rajput et al. (2021)
1 more