› 8ea2

X-ray diffraction
2.39Å resolution

Structure of 2-hydroxyisoflavanone dehydratase from Pueraria lobate

Released:
DOI: 10.2210/pdb8ea2/pdb
PDB entry 8ea2 coloured by chain, front view.
PDB entry 8ea2 coloured by chain, side view.
PDB entry 8ea2 coloured by chain, top view.
Source organism: Pueraria montana var. lobata
Primary publication:
The protein conformational basis of isoflavone biosynthesis.
Wang X, Pan H, Sagurthi S, Paris V, Zhuo C, Dixon RA
Commun Biol 5 1249 (2022)
PMID: 36376429

Function and Biology Details

Reaction catalysed: 
2,4',5,7-tetrahydroxyisoflavanone = genistein + H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123179 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha/beta hydrolase fold-3 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 353 amino acids
Theoretical weight: 38.92 KDa
Source organism: Pueraria montana var. lobata
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: E9M5G1 (Residues: 1-325; Coverage: 100%)
Gene name: 2-HID
Sequence domains: alpha/beta hydrolase fold

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P3121
Unit cell:
a: 102.309Å b: 102.309Å c: 70.239Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.186 0.243
Expression system: Escherichia coli BL21(DE3)

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