1z2u

X-ray diffraction
1.1Å resolution

The 1.1A crystallographic structure of ubiquitin-conjugating enzyme (ubc-2) from Caenorhabditis elegans: functional and evolutionary significance

Released:
Source organism: Caenorhabditis elegans
Entry authors: Gavira JA, DiGiamamarino E, Tempel W, Liu ZJ, Wang BC, Meehan E, Ng JD, 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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-152802 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin-conjugating enzyme E2 2 Chain: A
Molecule details ›
Chain: A
Length: 150 amino acids
Theoretical weight: 17.01 KDa
Source organism: Caenorhabditis elegans
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P35129 (Residues: 1-147; Coverage: 100%)
Gene names: M7.1, let-70, ubc-2
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21
Unit cell:
a: 29.604Å b: 60.457Å c: 43.98Å
α: 90° β: 106.45° γ: 90°
R-values:
R R work R free
0.132 0.13 0.149
Expression system: Escherichia coli BL21(DE3)