› 1yj1

X-ray diffraction
1.3Å resolution

X-ray Crystal Structure of a Chemically Synthesized [D-Gln35]Ubiquitin

Released:
DOI: 10.2210/pdb1yj1/pdb
PDB entry 1yj1 coloured by chain, front view.
PDB entry 1yj1 coloured by chain, side view.
PDB entry 1yj1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Total chemical synthesis and X-ray crystal structure of a protein diastereomer: [D-Gln 35]ubiquitin.
Bang D, Makhatadze GI, Tereshko V, Kossiakoff AA, Kent SB
Angew Chem Int Ed Engl 44 3852-6 (2005)
PMID: 15834850

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo trimer
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-162564 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 76 amino acids
Theoretical weight: 8.63 KDa
Source organism: Homo sapiens
Expression system: Not provided
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

2 bound ligands:
Ligand CD 17 x CD
Ligand CL 3 x CL
1 modified residue:
Ligand DGN 3 x DGN

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 43.872Å b: 50.395Å c: 92.941Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.195 0.218
Expression system: Not provided

Quick links

Citations

12 review citations

Chemoselective ligation and modification strategies for peptides and proteins.
Hackenberger et al. (2008)
11 more

6 mentions without citation

Protein backbone and sidechain torsion angles predicted from NMR chemical shifts using artificial neural networks.
Shen et al. (2013)
5 more