1pzv

X-ray diffraction
2.52Å resolution

Crystal structures of two UBC (E2) enzymes of the ubiquitin-conjugating system in Caenorhabditis elegans

Released:
Source organism: Caenorhabditis elegans
Entry authors: Schormann N, Lin G, Li S, Symersky J, Qiu S, Finley J, Luo D, Stanton A, Carson M, Luo M, Southeast Collaboratory for Structural Genomics (SECSG)

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
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-152707 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable ubiquitin-conjugating enzyme E2 7 Chain: A
Molecule details ›
Chain: A
Length: 164 amino acids
Theoretical weight: 18.96 KDa
Source organism: Caenorhabditis elegans
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P34477 (Residues: 1-164; Coverage: 100%)
Gene names: F58A4.10, ubc-7
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: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 48.474Å b: 52.184Å c: 68.882Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.252 0.241 0.289
Expression system: Escherichia coli BL21(DE3)