PDBe 4ii3

X-ray diffraction
2.9Å resolution

Crystal structure of S. pombe Ubiquitin activating enzyme 1 (Uba1) in complex with ubiquitin and ATP/Mg

Released:
Primary publication:
Structure of a ubiquitin e1-e2 complex: insights to e1-e2 thioester transfer.
Mol. Cell 49 884-96 (2013)
PMID: 23416107

Function and Biology Details

Reaction catalysed:
ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin Chains: B, D
Molecule details ›
Chains: B, D
Length: 96 amino acids
Theoretical weight: 10.74 KDa
Source organism: Schizosaccharomyces pombe 972h-
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0CH07 (Residues: 1-76; Coverage: 59%)
Gene names: SPAC1805.12c, ubi2, uep1
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P21212
Unit cell:
a: 180.5Å b: 113.3Å c: 126.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.239 0.239 0.283
Expression system: Escherichia coli BL21(DE3)