PDBe 5bnb

X-ray diffraction
2.49Å resolution

Crystal structure of a Ube2S-ubiquitin conjugate

Released:
Source organism: Homo sapiens
Primary publication:
Crystal Structure of a Ube2S-Ubiquitin Conjugate.
OpenAccess logo PLoS ONE 11 e0147550 (2016)
PMID: 26828794

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
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin-conjugating enzyme E2 S Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 156 amino acids
Theoretical weight: 17.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q16763 (Residues: 1-156; Coverage: 70%)
Gene names: E2EPF, OK/SW-cl.73, UBE2S
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme
Ubiquitin Chains: E, F, G, I
Molecule details ›
Chains: E, F, G, I
Length: 76 amino acids
Theoretical weight: 8.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0CG47 (Residues: 153-228; Coverage: 33%)
Gene name: UBB
Sequence domains: Ubiquitin family

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P21
Unit cell:
a: 94.906Å b: 45.854Å c: 110.576Å
α: 90° β: 93.14° γ: 90°
R-values:
R R work R free
0.246 0.243 0.304
Expression system: Escherichia coli BL21(DE3)