3icu

X-ray diffraction
2.1Å resolution

Protease-associated domain of the E3 ligase grail

Released:
Source organism: Homo sapiens
Entry authors: Walker JR, Yermekbayeva L, Seitova A, Weigelt J, Bountra C, Arrowsmith CH, Edwards AM, Bochkarev A, Dhe-Paganon S, Structural Genomics Consortium (SGC)

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
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-186240 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase RNF128 Chain: A
Molecule details ›
Chain: A
Length: 194 amino acids
Theoretical weight: 21.05 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q8TEB7 (Residues: 38-204; Coverage: 43%)
Gene name: RNF128
Sequence domains: PA domain
Structure domains: Glucose Oxidase; domain 1

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P43212
Unit cell:
a: 65.795Å b: 65.795Å c: 136.524Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.195 0.218
Expression system: Spodoptera frugiperda