2RTU: Oxidized human HMGB1 A box

Solution structure of oxidized human HMGB1 A box. Determined by solution NMR. Released 5 Mar 2014.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
706
Mol. weight
10.12 kDa
Released
5 Mar 2014

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

Secondary structure: helices and β-sheets

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.

Chain A: 5 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix2-43
α-helix18-3316
α-helix41-5212
α-helix57-6913
α-helix71-788

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
High mobility group protein B1Aprotein87Homo sapiensP09429 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2RTU_1 High mobility group protein B1 (chains A)
GSHMGKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSERWKTMSAKEK
GKFEDMAKADKARYEREMKTYIPPKGE

Primary citation

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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