5ojj

X-ray diffraction
1.85Å resolution

Crystal structure of the Zn-bound ubiquitin-conjugating enzyme Ube2T

Released:

Function and Biology Details

Reaction catalysed:
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-192478 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin-conjugating enzyme E2 T Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 154 amino acids
Theoretical weight: 17.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9NPD8 (Residues: 1-154; Coverage: 78%)
Gene names: HSPC150, PIG50, UBE2T
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P21
Unit cell:
a: 56.02Å b: 96.383Å c: 89.996Å
α: 90° β: 93.28° γ: 90°
R-values:
R R work R free
0.179 0.178 0.199
Expression system: Escherichia coli BL21