› 2pru

Solution NMR

NMR Structure of Human apoS100B at 10C

Released:
DOI: 10.2210/pdb2pru/pdb
PDB entry 2pru coloured by chain, ensemble of 20 models, front view.
PDB entry 2pru coloured by chain, ensemble of 20 models, side view.
PDB entry 2pru coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Analysis of the structure of human apo-S100B at low temperature indicates a unimodal conformational distribution is adopted by calcium-free S100 proteins.
Malik S, Revington M, Smith SP, Shaw GS
Proteins 73 28-42 (2008)
PMID: 18384084

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137551 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein S100-B Chains: A, B
Molecule details ›
Chains: A, B
Length: 91 amino acids
Theoretical weight: 10.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04271 (Residues: 2-92; Coverage: 99%)
Gene name: S100B
Sequence domains:
Structure domains: EF-hand

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: CNS - non-crystallograqphic symmetry for the homodimer, distance geometry, simulated annealing, molecular dynamics. Final Refinement in the presence of explicit solvent.
Expression system: Escherichia coli

Quick links

Citations

3 review citations

S100-annexin complexes--structural insights.
Rintala-Dempsey et al. (2008)
2 more

3 mentions without citation

Calprotectin S100A9 calcium-binding loops I and II are essential for keratinocyte resistance to bacterial invasion.
Champaiboon et al. (2009)
2 more