2wqg

Solution NMR

SAP domain from Tho1: L31W (fluorophore) mutant

Released:
Source organism: Saccharomyces cerevisiae
Primary publication:
Engineering a two-helix bundle protein for folding studies.
OpenAccess logo Protein Eng. Des. Sel. 23 357-64 (2010)
PMID: 20130106

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein THO1 Chain: A
Molecule details ›
Chain: A
Length: 51 amino acids
Theoretical weight: 5.66 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P40040 (Residues: 2-50; Coverage: 23%)
Gene names: THO1, YER063W
Sequence domains: SAP domain
Structure domains: SAP domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: MANUAL ASSIGNMENT THEN SIMULATED ANNEALING
Expression system: Escherichia coli BL21(DE3)