› 4c9z

X-ray diffraction
1.95Å resolution

Crystal structure of Siah1 at 1.95 A resolution

Released:
DOI: 10.2210/pdb4c9z/pdb
PDB entry 4c9z coloured by chain, front view.
PDB entry 4c9z coloured by chain, side view.
PDB entry 4c9z coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Two high-resolution structures of the human E3 ubiquitin ligase Siah1.
Rimsa V, Eadsforth TC, Hunter WN
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:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184857 (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: Q8IUQ4 (Residues: 91-282; Coverage: 68%)
Gene names: HUMSIAH, SIAH1
Sequence domains:
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand ZN 4 x ZN
Ligand CL 4 x CL
Ligand GOL 3 x GOL
Ligand SO4 3 x SO4
Ligand TRS 2 x TRS
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)

Quick links

Citations

4 citation in other articles

The SIAH E3 ubiquitin ligases promote Wnt/β-catenin signaling through mediating Wnt-induced Axin degradation.
Ji et al. (2017)
3 more

3 mentions without citation

Modeling beta-sheet peptide-protein interactions: Rosetta FlexPepDock in CAPRI rounds 38-45.
Khramushin et al. (2020)
2 more