› 2rtu

Solution NMR

Solution structure of oxidized human HMGB1 A box

Released:
DOI: 10.2210/pdb2rtu/pdb
PDB entry 2rtu coloured by chain, ensemble of 20 models, front view.
PDB entry 2rtu coloured by chain, ensemble of 20 models, side view.
PDB entry 2rtu coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
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, Uewaki J, Kobayashi N, Tate S
Biochem Biophys Res Commun 441 701-6 (2013)
PMID: 24427810

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140653 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
High mobility group protein B1 Chain: A
Molecule details ›
Chain: A
Length: 87 amino acids
Theoretical weight: 10.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09429 (Residues: 1-84; Coverage: 39%)
Gene names: HMG1, HMGB1
Sequence domains: HMG-box domain
Structure domains: High mobility group box domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 91%
Refinement method: torsion angle dynamics, simulated annealing
Expression system: Escherichia coli

Quick links

Citations

5 review citations

HMGB1 in health and disease.
Kang et al. (2014)
4 more

8 mentions without citation

Thiol-Disulfide Exchange Reactions in the Mammalian Extracellular Environment.
Yi et al. (2016)
7 more