› 2a26

X-ray diffraction
1.2Å resolution

Crystal structure of the N-terminal, dimerization domain of Siah Interacting Protein

Released:
DOI: 10.2210/pdb2a26/pdb
PDB entry 2a26 coloured by chain, front view.
PDB entry 2a26 coloured by chain, side view.
PDB entry 2a26 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural analysis of Siah1-Siah-interacting protein interactions and insights into the assembly of an E3 ligase multiprotein complex.
Santelli E, Leone M, Li C, Fukushima T, Preece NE, Olson AJ, Ely KR, Reed JC, Pellecchia M, Liddington RC, Matsuzawa S
J Biol Chem 280 34278-87 (2005)
PMID: 16085652

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-190737 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Calcyclin-binding protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 50 amino acids
Theoretical weight: 5.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9HB71 (Residues: 1-47; Coverage: 21%)
Gene names: CACYBP, PNAS-107, S100A6BP, SIP
Sequence domains: Siah interacting protein, N terminal
Structure domains: UVR domain

Ligands and Environments

2 bound ligands:
Ligand SO4 1 x SO4
Ligand CXS 1 x CXS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1, SSRL BEAMLINE BL9-2
Spacegroup: C2221
Unit cell:
a: 58.793Å b: 152.609Å c: 36.988Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.174 0.198
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

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

4 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)
3 more