2a25

X-ray diffraction
2.2Å resolution

Crystal structure of Siah1 SBD bound to the peptide EKPAAVVAPITTG from SIP

Released:

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:
Cellular component:

Structure analysis Details

Assembly composition:
Non-polymer only tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase SIAH1 Chain: A
Molecule details ›
Chain: A
Length: 193 amino acids
Theoretical weight: 21.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8IUQ4 (Residues: 90-282; Coverage: 68%)
Gene names: HUMSIAH, SIAH1
Structure domains:
Calcyclin-binding protein Chain: B
Molecule details ›
Chain: B
Length: 13 amino acids
Theoretical weight: 1.25 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q9HB71 (Residues: 58-70; Coverage: 6%)
Gene names: CACYBP, PNAS-107, S100A6BP, SIP

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E
Spacegroup: C2221
Unit cell:
a: 47.635Å b: 107.761Å c: 78.414Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.213 0.252
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided