› 6thu

X-ray diffraction
2.6Å resolution

Crystal structure of the SVS_A2 protein (A224I mutant) from ancestral sequence reconstruction at 2.6 A resolution

Released:
DOI: 10.2210/pdb6thu/pdb
PDB entry 6thu coloured by chain, front view.
PDB entry 6thu coloured by chain, side view.
PDB entry 6thu coloured by chain, top view.
Source organism: Streptomyces sp. CWA1
Primary publication:
Engineering of Ancestors as a Tool to Elucidate Structure, Mechanism, and Specificity of Extant Terpene Cyclase.
Schriever K, Saenz-Mendez P, Rudraraju RS, Hendrikse NM, Hudson EP, Biundo A, Schnell R, Syrén PO
OpenAccess logo J Am Chem Soc 143 3794-3807 (2021)
PMID: 33496585

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-167510 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
SVS_AS10 variant Chains: A, B
Molecule details ›
Chains: A, B
Length: 361 amino acids
Theoretical weight: 40.52 KDa
Source organism: Streptomyces sp. CWA1
Expression system: Escherichia coli

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX IV BEAMLINE BioMAX
Spacegroup: P212121
Unit cell:
a: 74.91Å b: 105.094Å c: 108.253Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.19 0.216
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Engineering functional thermostable proteins using ancestral sequence reconstruction.
Thomson et al. (2022)
4 more

1 mention without citation

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