2ct2

Solution NMR

Solution Structure of the RING domain of the Tripartite motif protein 32

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

Function and Biology Details

Reaction catalysed:
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-171518 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase TRIM32 Chain: A
Molecule details ›
Chain: A
Length: 88 amino acids
Theoretical weight: 9.49 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q13049 (Residues: 10-84; Coverage: 12%)
Gene names: HT2A, TRIM32
Sequence domains: RING-type zinc-finger
Structure domains: Zinc/RING finger domain, C3HC4 (zinc finger)

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Not provided