› 1qyc

X-ray diffraction
2.2Å resolution

Crystal structures of pinoresinol-lariciresinol and phenylcoumaran benzylic ether reductases, and their relationship to isoflavone reductases

Released:
DOI: 10.2210/pdb1qyc/pdb
PDB entry 1qyc coloured by chain, front view.
PDB entry 1qyc coloured by chain, side view.
PDB entry 1qyc coloured by chain, top view.
Source organism: Pinus taeda
Primary publication:
Crystal structures of pinoresinol-lariciresinol and phenylcoumaran benzylic ether reductases and their relationship to isoflavone reductases.
Min T, Kasahara H, Bedgar DL, Youn B, Lawrence PK, Gang DR, Halls SC, Park H, Hilsenbeck JL, Davin LB, Lewis NG, Kang C
J Biol Chem 278 50714-23 (2003)
PMID: 13129921

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192285 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phenylcoumaran benzylic ether reductase PT1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 308 amino acids
Theoretical weight: 33.56 KDa
Source organism: Pinus taeda
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9LL41 (Residues: 1-308; Coverage: 100%)
Gene name: PCBER
Sequence domains: NmrA-like family
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P21
Unit cell:
a: 66.195Å b: 67.941Å c: 75.019Å
α: 90° β: 115.08° γ: 90°
R-values:
R R work R free
0.249 0.195 0.242
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

The Origin and Evolution of Plant Flavonoid Metabolism.
Yonekura-Sakakibara et al. (2019)
3 more

2 mentions without citation

Structure and function of enzymes involved in the biosynthesis of phenylpropanoids.
Ferrer et al. (2008)
1 more