2WQG: SAP domain from Tho1: L31W (fluorophore) mutant

SAP domain from Tho1: L31W (fluorophore) mutant. Determined by solution NMR. Released 16 Feb 2010.

Method
Solution NMR
Organism
SACCHAROMYCES CEREVISIAE
Chains
1
Atoms
397
Mol. weight
5.66 kDa
Released
16 Feb 2010

Explore 2WQG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2WQG contains 2 α-helices and 0 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 2 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix10-2011
α-helix28-4013

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein THO1Aprotein51SACCHAROMYCES CEREVISIAEP40040 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2WQG_1 PROTEIN THO1 (chains A)
GSADYSSLTVVQLKDLLTKRNLSVGGLKNEWVQRLIKDDEESKGESEVSPQ

Primary citation

Engineering a Two-Helix Bundle Protein for Folding Studies. Dodson, C.A., Ferguson, N., Rutherford, T.J. et al. Protein Eng Des Sel (2010) 23:357. DOI 10.1093/PROTEIN/GZP080 · PubMed

Other PDB entries of the same protein (UniProt P40040 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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