› 5l86

X-ray diffraction
1.9Å resolution

engineered ascorbate peroxidise

Released:
DOI: 10.2210/pdb5l86/pdb
PDB entry 5l86 coloured by chain, front view.
PDB entry 5l86 coloured by chain, side view.
PDB entry 5l86 coloured by chain, top view.
Source organism: Glycine max
Primary publication:
A Chemically Programmed Proximal Ligand Enhances the Catalytic Properties of a Heme Enzyme.
Green AP, Hayashi T, Mittl PR, Hilvert D
J Am Chem Soc 138 11344-52 (2016)
PMID: 27500802

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:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174997 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-ascorbate peroxidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 247 amino acids
Theoretical weight: 26.81 KDa
Source organism: Glycine max
Expression system: Escherichia coli
UniProt:
  • Canonical: Q43758 (Residues: 3-249; Coverage: 99%)
Gene name: apx1
Sequence domains: Peroxidase
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
1 bound ligand:
Ligand SO4 6 x SO4
1 modified residue:
Ligand MHS 2 x MHS

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 84.46Å b: 81.95Å c: 69.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.179 0.231
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Biocatalysis with Unnatural Amino Acids: Enzymology Meets Xenobiology.
Agostini et al. (2017)
7 more