PDBe 3cmm

X-ray diffraction
2.7Å resolution

Crystal Structure of the Uba1-Ubiquitin Complex

Released:

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: 76 amino acids
Theoretical weight: 8.57 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0CG63 (Residues: 305-380; Coverage: 20%)
Gene names: SCD2, UBI4, YLL039C
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Ubiquitin-activating enzyme E1 1 Chains: A, C
Molecule details ›
Chains: A, C
Length: 1015 amino acids
Theoretical weight: 113.52 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P22515 (Residues: 10-1024; Coverage: 99%)
Gene names: UBA1, YKL210W
Sequence domains:
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P212121
Unit cell:
a: 115.363Å b: 118.564Å c: 207.567Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.191 0.247
Expression systems:
  • Escherichia coli BL21(DE3)
  • Escherichia coli