› 5tdx

X-ray diffraction
1.96Å resolution

Resurrected Ancestral Hydroxynitrile Lyase from Flowering Plants

Released:
DOI: 10.2210/pdb5tdx/pdb
PDB entry 5tdx coloured by chain, front view.
PDB entry 5tdx coloured by chain, side view.
PDB entry 5tdx coloured by chain, top view.
Source organism: synthetic construct
Primary publication:
Larger active site in an ancestral hydroxynitrile lyase increases catalytically promiscuous esterase activity.
Jones BJ, Evans RL, Mylrea NJ, Chaudhury D, Luo C, Guan B, Pierce CT, Gordon WR, Wilmot CM, Kazlauskas RJ
PLoS One 15 e0235341 (2020)
PMID: 32603354

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-166110 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ancestral Hydroxynitrile Lyase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 272 amino acids
Theoretical weight: 31.12 KDa
Source organism: synthetic construct
Expression system: Escherichia coli BL21(DE3)
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand GOL 6 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P43212
Unit cell:
a: 108.265Å b: 108.265Å c: 201.188Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.177 0.226
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 citation in other articles

Engineering of Ancestors as a Tool to Elucidate Structure, Mechanism, and Specificity of Extant Terpene Cyclase.
Schriever et al. (2021)
2 more

2 mentions without citation

Larger active site in an ancestral hydroxynitrile lyase increases catalytically promiscuous esterase activity.
Jones et al. (2020)
1 more