4oyj

X-ray diffraction
3Å resolution

Structure of the apo HOIP PUB domain

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:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-188461 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase RNF31 Chains: A, B, C, D, E, F, G, H, I, J, K, L, M
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M
Length: 186 amino acids
Theoretical weight: 21.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96EP0 (Residues: 1-184; Coverage: 17%)
Gene names: RNF31, ZIBRA
Sequence domains:
Structure domains: Methane Monooxygenase Hydroxylase; Chain G, domain 1

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: C2
Unit cell:
a: 155.19Å b: 99.54Å c: 173.73Å
α: 90° β: 99.9° γ: 90°
R-values:
R R work R free
0.209 0.207 0.254
Expression system: Escherichia coli BL21(DE3)