› 1k2f

X-ray diffraction
2.6Å resolution

siah, Seven In Absentia Homolog

Released:
DOI: 10.2210/pdb1k2f/pdb
PDB entry 1k2f coloured by chain, front view.
PDB entry 1k2f coloured by chain, side view.
PDB entry 1k2f coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Siah ubiquitin ligase is structurally related to TRAF and modulates TNF-alpha signaling.
Polekhina G, House CM, Traficante N, Mackay JP, Relaix F, Sassoon DA, Parker MW, Bowtell DD
Nat Struct Biol 9 68-75 (2002)
PMID: 11742346

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 domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158218 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase SIAH1A Chains: A, B
Molecule details ›
Chains: A, B
Length: 190 amino acids
Theoretical weight: 21.42 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P61092 (Residues: 93-282; Coverage: 67%)
Gene name: Siah1a
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 6 x ZN
Ligand BME 4 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 66.474Å b: 73.966Å c: 80.554Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.22 0.277
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

RING domain E3 ubiquitin ligases.
Deshaies et al. (2009)
7 more

3 mentions without citation

Overview of protein structural and functional folds.
Sun et al. (2004)
2 more