› 8dju

X-ray diffraction
1.5Å resolution

Cytosolic ascorbate peroxidase from Sorghum bicolor - bicyclic dehydroascorbic acid complex

Released:
DOI: 10.2210/pdb8dju/pdb
PDB entry 8dju coloured by chain, front view.
PDB entry 8dju coloured by chain, side view.
PDB entry 8dju coloured by chain, top view.
Source organism: Sorghum bicolor
Primary publication:
A sorghum ascorbate peroxidase with four binding sites has activity against ascorbate and phenylpropanoids.
Zhang B, Lewis JA, Vermerris W, Sattler SE, Kang C
Plant Physiol (2022)
PMID: 36575825

Function and Biology Details

Reaction catalysed: 
(1a) 2 L-ascorbate + H(2)O(2) + 2 H(+) = 2 monodehydroascorbate + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-215644 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-ascorbate peroxidase Chain: A
Molecule details ›
Chain: A
Length: 250 amino acids
Theoretical weight: 27.25 KDa
Source organism: Sorghum bicolor
Expression system: Escherichia coli
UniProt:
  • Canonical: C5WNL8 (Residues: 1-250; Coverage: 100%)
Gene name: SORBI_3001G410200
Sequence domains: Peroxidase

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
3 bound ligands:
Ligand SO4 1 x SO4
Ligand SIV 1 x SIV
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P212121
Unit cell:
a: 38.19Å b: 75.303Å c: 83.385Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.134 0.133 0.153
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Novel insight into functions of ascorbate peroxidase in higher plants: More than a simple antioxidant enzyme.
Li S. (2023)
2 other articles