5ljn

X-ray diffraction
2.7Å resolution

Structure of the HOIP PUB domain bound to SPATA2 PIM peptide

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, B
Molecule details ›
Chains: A, B
Length: 173 amino acids
Theoretical weight: 19.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96EP0 (Residues: 5-176; Coverage: 16%)
Gene names: RNF31, ZIBRA
Sequence domains: PUB domain
Structure domains: Methane Monooxygenase Hydroxylase; Chain G, domain 1
Spermatogenesis-associated protein 2 Chains: C, D
Molecule details ›
Chains: C, D
Length: 8 amino acids
Theoretical weight: 927 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q9UM82 (Residues: 334-341; Coverage: 2%)
Gene names: KIAA0757, PD1, SPATA2

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P43
Unit cell:
a: 89.04Å b: 89.04Å c: 53.563Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.235 0.232 0.28
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided