PDBe 4c9z

X-ray diffraction
1.95Å resolution

Crystal structure of Siah1 at 1.95 A resolution

Released:
Source organism: Homo sapiens
Primary publication:
Two high-resolution structures of the human E3 ubiquitin ligase Siah1.
OpenAccess logo Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 69 1339-43 (2013)
PMID: 24316825

Function and Biology Details

Reaction catalysed:
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase SIAH1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 195 amino acids
Theoretical weight: 21.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: NEW Q8IUQ4 (Residues: 91-282; Coverage: 68%)
Gene names: HUMSIAH, SIAH1
Structure domains:

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: I222
Unit cell:
a: 75.14Å b: 104.59Å c: 133.16Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.198 0.239
Expression system: Escherichia coli BL21(DE3)