› 9g0l

X-ray diffraction
1.9Å resolution

Crystal structure of the RING-ZnF1 fragment of SIAH1

Released:
DOI: 10.2210/pdb9g0l/pdb
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PDB entry 9g0l coloured by chain, front view.
PDB entry 9g0l coloured by chain, side view.
PDB entry 9g0l coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
RING dimerisation drives higher-order organisation of SINA/SIAH E3 ubiquitin ligases.
Coste F, Mishra A, Chapuis C, Mance L, Pukało Z, Bigot N, Goffinont S, Gaudon V, Garnier N, Talhaoui I, Castaing B, Huet S, Suskiewicz MJ
FEBS J (2025)
PMID: 39910688

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)
Assembly name:
PDBe Complex ID:
PDB-CPX-184857 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase SIAH1 Chain: A
Molecule details ›
Chain: A
Length: 107 amino acids
Theoretical weight: 11.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8IUQ4 (Residues: 28-125; Coverage: 35%)
Gene names: HUMSIAH, SIAH1
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 3 x ZN
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P43212
Unit cell:
a: 69.85Å b: 69.85Å c: 62.713Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.202 0.237
Expression system: Escherichia coli

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