2ct7

Solution NMR

Solution Structure of the IBR domain of the RING finger protein 31 protein

Released:
Source organism: Homo sapiens
Entry authors: Miyamoto K, Koshiba S, Tomizawa T, Inoue M, Kigawa T, Yokoyama S, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase RNF31 Chain: A
Molecule details ›
Chain: A
Length: 86 amino acids
Theoretical weight: 9.95 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q96EP0 (Residues: 779-851; Coverage: 7%)
Gene names: RNF31, ZIBRA
Sequence domains: IBR domain, a half RING-finger domain

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 87%
Refinement method: torsion angle dynamics
Chemical shifts: BMR11321  
Expression system: Not provided