3hm3

X-ray diffraction
1.96Å resolution

The Structure and conformation of Lys-63 linked tetra-ubiquitin

Released:
Source organism: Homo sapiens
Primary publication:
The structure and conformation of Lys63-linked tetraubiquitin.
J Mol Biol 392 1117-24 (2009)
PMID: 19664638

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143327 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 76 amino acids
Theoretical weight: 8.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG48 (Residues: 609-684; Coverage: 11%)
Gene name: UBC
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P213
Unit cell:
a: 105.882Å b: 105.882Å c: 105.882Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.186 0.236
Expression system: Escherichia coli