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Solution NMR

Structural changes induced in apo-s100a1 protein by the disulphide formation between its CYS85 residue and b-mercaptoethanol

Released:
DOI: 10.2210/pdb2jpt/pdb
PDB entry 2jpt coloured by chain, ensemble of 10 models, front view.
PDB entry 2jpt coloured by chain, ensemble of 10 models, side view.
PDB entry 2jpt coloured by chain, ensemble of 10 models, top view.
Source organism: Bos taurus
Primary publication:
Structural and motional changes induced in apo-S100A1 protein by the disulfide formation between its Cys 85 residue and beta-mercaptoethanol.
Zhukov I, Ejchart A, Bierzyński A
Biochemistry 47 640-50 (2008)
PMID: 18088104

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-135978 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein S100-A1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 93 amino acids
Theoretical weight: 10.4 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P02639 (Residues: 2-94; Coverage: 99%)
Gene name: S100A1
Sequence domains:
Structure domains: EF-hand

Ligands and Environments

1 bound ligand:
Ligand BME 2 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Escherichia coli

Quick links

Citations

3 review citations

S100A1 in cardiovascular health and disease: closing the gap between basic science and clinical therapy.
Kraus et al. (2009)
2 more

3 mentions without citation

Conservation of Specificity in Two Low-Specificity Proteins.
Wheeler et al. (2018)
2 more