› 4pih

X-ray diffraction
1.5Å resolution

X-ray crystal structure of the K33S mutant of ubiquitin

Released:
DOI: 10.2210/pdb4pih/pdb
PDB entry 4pih coloured by chain, front view.
PDB entry 4pih coloured by chain, side view.
PDB entry 4pih coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Enhancing ubiquitin crystallization through surface-entropy reduction.
Loll PJ, Xu P, Schmidt JT, Melideo SL
Acta Crystallogr F Struct Biol Commun 70 1434-42 (2014)
PMID: 25286958

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-158832 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin Chains: A, B
Molecule details ›
Chains: A, B
Length: 76 amino acids
Theoretical weight: 8.53 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62987 (Residues: 1-76; Coverage: 59%)
Gene names: UBA52, UBCEP2
Sequence domains: Ubiquitin family

Ligands and Environments

2 bound ligands:
Ligand CA 3 x CA
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P1
Unit cell:
a: 27.35Å b: 32.74Å c: 40.34Å
α: 69.77° β: 72.55° γ: 73.12°
R-values:
R R work R free
0.168 0.165 0.19
Expression system: Escherichia coli

Quick links

Citations

3 mentions without citation

Systematic analysis of residual density suggests that a major limitation in well-refined X-ray structures of proteins is the omission of ordered solvent.
Wang J. (2017)
2 more