5h9m

X-ray diffraction
1.76Å resolution

Crystal structure of siah2 SBD domain

Released:
Source organism: Homo sapiens
Entry authors: Dong A, Zhang Q, Walker JR, Bountra C, Arrowsmith CH, Edwards AM, Tong Y, Structural Genomics Consortium (SGC)

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:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-128877 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase SIAH2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 192 amino acids
Theoretical weight: 21.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O43255 (Residues: 131-321; Coverage: 59%)
Gene name: SIAH2
Sequence domains:
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 53.624Å b: 68.753Å c: 102.884Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.178 0.227
Expression system: Escherichia coli BL21(DE3)