5x0w

X-ray diffraction
3Å resolution

Molecular mechanism for the binding between Sharpin and HOIP

Released:

Function and Biology Details

Reaction catalysed:
(1a) [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [RBR-type E3 ubiquitin transferase]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [RBR-type E3 ubiquitin transferase]-S-ubiquitinyl-L-cysteine
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase RNF31 Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 166 amino acids
Theoretical weight: 18.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96EP0 (Residues: 480-639; Coverage: 15%)
Gene names: RNF31, ZIBRA
Sequence domains: HOIP UBA domain pair
Sharpin Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 108 amino acids
Theoretical weight: 11.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H0F6 (Residues: 206-309; Coverage: 27%)
Gene names: PSEC0216, SHARPIN, SIPL1

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P32
Unit cell:
a: 101.347Å b: 101.347Å c: 146.982Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.263 0.261 0.302
Expression system: Escherichia coli