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Solution NMR

THE STRUCTURE OF CALCYCLIN REVEALS A NOVEL HOMODIMERIC FOLD FOR S100 CA2+-BINDING PROTEINS, NMR, 22 STRUCTURES

Released:
DOI: 10.2210/pdb1cnp/pdb
PDB entry 1cnp coloured by chain, ensemble of 22 models, front view.
PDB entry 1cnp coloured by chain, ensemble of 22 models, side view.
PDB entry 1cnp coloured by chain, ensemble of 22 models, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
The structure of calcyclin reveals a novel homodimeric fold for S100 Ca(2+)-binding proteins.
Potts BC, Smith J, Akke M, Macke TJ, Okazaki K, Hidaka H, Case DA, Chazin WJ
Nat Struct Biol 2 790-6 (1995)
PMID: 7552751

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151802 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein S100-A6 Chains: A, B
Molecule details ›
Chains: A, B
Length: 90 amino acids
Theoretical weight: 10.17 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: P30801 (Residues: 1-90; Coverage: 100%)
Gene name: S100A6
Sequence domains: S-100/ICaBP type calcium binding domain
Structure domains: EF-hand

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores

Quick links

Citations

24 review citations

The S100 family of EF-hand calcium-binding proteins: functions and pathology.
Schäfer et al. (1996)
23 more

2 mentions without citation

Predicting data quality in biological X-ray solution scattering.
Wang et al. (2018)
1 more