4juy

X-ray diffraction
2.4Å resolution

Crystal structure of the PUB domain of E3 ubiquitin ligase RNF31

Released:
Source organism: Homo sapiens
Entry authors: Dong A, Hu J, Li Y, Wernimont A, Bountra C, Arrowsmith CH, Edwards AM, Tong Y, Structural Genomics Consortium (SGC)

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:
homo octamer (preferred)
PDBe Complex ID:
PDB-CPX-188471 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase RNF31 Chains: A, B
Molecule details ›
Chains: A, B
Length: 198 amino acids
Theoretical weight: 22.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q96EP0 (Residues: 1-180; 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: APS BEAMLINE 19-ID
Spacegroup: F432
Unit cell:
a: 256.488Å b: 256.488Å c: 256.488Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.237 0.236 0.258
Expression system: Escherichia coli BL21