PDBe 5knl

X-ray diffraction
2.5Å resolution

Crystal structure of S. pombe ubiquitin E1 (Uba1) in complex with Ubc15 and ubiquitin

Released:

Function and Biology Details

Reactions catalysed:
ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
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:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Ubiquitin-60S ribosomal protein L40 fusion protein Chains: B, E
Molecule details ›
Chains: B, E
Length: 96 amino acids
Theoretical weight: 10.9 KDa
Source organism: Moesziomyces antarcticus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A081CEG8 (Residues: 1-76; Coverage: 59%)
Gene name: PAN0_007c3281
Sequence domains: Ubiquitin family
Ubiquitin-conjugating enzyme E2 15 Chains: C, F
Molecule details ›
Chains: C, F
Length: 175 amino acids
Theoretical weight: 20.2 KDa
Source organism: Schizosaccharomyces pombe 972h-
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9Y818 (Residues: 1-167; Coverage: 100%)
Gene names: SPBC1105.09, ubc15
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P1
Unit cell:
a: 77.111Å b: 82.238Å c: 135.376Å
α: 102.1° β: 95.78° γ: 90.86°
R-values:
R R work R free
0.22 0.216 0.251
Expression system: Escherichia coli BL21(DE3)