› 1qcq

X-ray diffraction
2.7Å resolution

UBIQUITIN CONJUGATING ENZYME

Released:
DOI: 10.2210/pdb1qcq/pdb
PDB entry 1qcq coloured by chain, front view.
PDB entry 1qcq coloured by chain, side view.
PDB entry 1qcq coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Tertiary structures of class I ubiquitin-conjugating enzymes are highly conserved: crystal structure of yeast Ubc4.
Cook WJ, Jeffrey LC, Xu Y, Chau V
Biochemistry 32 13809-17 (1993)
PMID: 8268156

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:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147473 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin-conjugating enzyme E2 4 Chain: A
Molecule details ›
Chain: A
Length: 148 amino acids
Theoretical weight: 16.47 KDa
Source organism: Saccharomyces cerevisiae
UniProt:
  • Canonical: P15731 (Residues: 1-148; Coverage: 100%)
Gene names: UBC4, YBR0745, YBR082C
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P41212
Unit cell:
a: 66.9Å b: 66.9Å c: 91.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.24 0.296

Quick links

Citations

4 review citations

Mechanisms underlying ubiquitination.
Pickart CM. (2001)
3 more

3 mentions without citation

Ubiquitin-binding domains.
Hurley et al. (2006)
2 more