› 1ayz

X-ray diffraction
2.6Å resolution

CRYSTAL STRUCTURE OF THE SACCHAROMYCES CEREVISIAE UBIQUITIN-CONJUGATING ENZYME RAD6 (UBC2) AT 2.6A RESOLUTION

Released:
DOI: 10.2210/pdb1ayz/pdb
PDB entry 1ayz coloured by chain, front view.
PDB entry 1ayz coloured by chain, side view.
PDB entry 1ayz coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Crystal structure of the Saccharomyces cerevisiae ubiquitin-conjugating enzyme Rad6 at 2.6 A resolution.
Worthylake DK, Prakash S, Prakash L, Hill CP
J Biol Chem 273 6271-6 (1998)
PMID: 9497353

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-138868 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin-conjugating enzyme E2 2 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 169 amino acids
Theoretical weight: 19.36 KDa
Source organism: Saccharomyces cerevisiae
UniProt:
  • Canonical: P06104 (Residues: 1-172; Coverage: 98%)
Gene names: RAD6, UBC2, YGL058W
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: NSLS BEAMLINE X12B
Spacegroup: I222
Unit cell:
a: 113.75Å b: 146.36Å c: 109.88Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.213 0.246

Quick links

Citations

8 review citations

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

13 mentions without citation

E2s: structurally economical and functionally replete.
Wenzel et al. (2011)
12 more