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X-ray diffraction
2.51Å resolution

Structure of Dehydroascrobate Reductase from Pennisetum Americanum in complex with two non-native ligands, Acetate in the G-site and Glycerol in the H-site

Released:
DOI: 10.2210/pdb5evo/pdb
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PDB entry 5evo coloured by chain, front view.
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PDB entry 5evo coloured by chain, top view.
Source organism: Cenchrus americanus
Primary publication:
Non-native ligands define the active site of Pennisetum glaucum (L.) R. Br dehydroascorbate reductase.
Krishna Das B, Kumar A, Maindola P, Mahanty S, Jain SK, Reddy MK, Arockiasamy A
Biochem Biophys Res Commun 473 1152-1157 (2016)
PMID: 27067046

Function and Biology Details

Reactions catalysed: 
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
RX + glutathione = HX + R-S-glutathione
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-197578 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dehydroascorbate reductase Chain: A
Molecule details ›
Chain: A
Length: 216 amino acids
Theoretical weight: 23.73 KDa
Source organism: Cenchrus americanus
Expression system: Escherichia coli
UniProt:
  • Canonical: U5XYA0 (Residues: 1-213; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ACT 1 x ACT
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P4322
Unit cell:
a: 69.494Å b: 69.494Å c: 111.557Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.196 0.241
Expression system: Escherichia coli

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Citations

2 review citations

Regulation of Ascorbate-Glutathione Pathway in Mitigating Oxidative Damage in Plants under Abiotic Stress.
Hasanuzzaman et al. (2019)
1 more

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