› 1ysm

Solution NMR

NMR Structure of N-terminal domain (Residues 1-77) of Siah-Interacting Protein.

Released:
DOI: 10.2210/pdb1ysm/pdb
PDB entry 1ysm coloured by chain, ensemble of 20 models, front view.
PDB entry 1ysm coloured by chain, ensemble of 20 models, side view.
PDB entry 1ysm coloured by chain, ensemble of 20 models, top view.
Source organism: Mus musculus
Primary publication:
The modular structure of SIP facilitates its role in stabilizing multiprotein assemblies.
Bhattacharya S, Lee YT, Michowski W, Jastrzebska B, Filipek A, Kuznicki J, Chazin WJ
Biochemistry 44 9462-71 (2005)
PMID: 15996101

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190022 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Calcyclin-binding protein Chain: A
Molecule details ›
Chain: A
Length: 77 amino acids
Theoretical weight: 8.79 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9CXW3 (Residues: 1-77; Coverage: 34%)
Gene names: Cacybp, Sip
Sequence domains: Siah interacting protein, N terminal
Structure domains: UVR domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: Torsion Angle Dynamics Simulated Annealing Restrained Molecular Dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

S100A6 binding protein and Siah-1 interacting protein (CacyBP/SIP): spotlight on properties and cellular function.
Schneider et al. (2011)
3 more

2 mentions without citation

Dimerization and phosphatase activity of calcyclin-binding protein/Siah-1 interacting protein: the influence of oxidative stress.
Topolska-Woś et al. (2015)
1 more