Solution structure of human sulfiredoxin (SRX). Determined by solution NMR. Released 19 Sept 2006.
Explore 2B6F in 3D Show helices and sheets RCSB PDB PDBe
2B6F contains 4 α-helices and 5 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 41-45 | 5 | 1 |
| α-helix | 46-48 | 3 | |
| β-strand | 49-50 | 2 | 1 |
| α-helix | 59-71 | 13 | |
| β-strand | 79-85 | 7 | 1 |
| β-strand | 91-95 | 5 | 1 |
| α-helix | 99-107 | 9 | |
| β-strand | 112-119 | 8 | 1 |
| α-helix | 122-129 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sulfiredoxin | A | protein | 121 | Homo sapiens | Q9BYN0 (AlphaFold model) |
>2B6F_1 Sulfiredoxin (chains A) GAPEGPGPSGGAQGGSIHSGRIAAVHNVPLSVLIRPLPSVLDPAKVQSLVDTIREDPDSV PPIDVLWIKGAQGGDYFYSFGGCHRYAAYQQLQRETIPAKLVQSTLSDLRVYLGASTPDL Q
Mutagenesis and Modeling of the Peroxiredoxin (Prx) Complex with the NMR Structure of ATP-Bound Human Sulfiredoxin Implicate Aspartate 187 of Prx I as the Catalytic Residue in ATP Hydrolysis. Lee, D.-Y., Park, S.J., Jeong, W. et al. Biochemistry (2006) 45:15301-15309. DOI 10.1021/bi061824h · PubMed
Other PDB entries of the same protein (UniProt Q9BYN0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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