Solution structure of oxidized human HMGB1 A box. Determined by solution NMR. Released 5 Mar 2014.
Explore 2RTU in 3D Show helices and sheets RCSB PDB PDBe
2RTU contains 5 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-4 | 3 | |
| α-helix | 18-33 | 16 | |
| α-helix | 41-52 | 12 | |
| α-helix | 57-69 | 13 | |
| α-helix | 71-78 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| High mobility group protein B1 | A | protein | 87 | Homo sapiens | P09429 (AlphaFold model) |
>2RTU_1 High mobility group protein B1 (chains A) GSHMGKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSERWKTMSAKEK GKFEDMAKADKARYEREMKTYIPPKGE
Redox-sensitive structural change in the A-domain of HMGB1 and its implication for the binding to cisplatin modified DNA. Wang, J., Tochio, N., Takeuchi, A. et al. Biochem Biophys Res Commun (2013) 441:701-706. PubMed
Other PDB entries of the same protein (UniProt P09429 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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