› 2kn5

Solution NMR

A Correspondence Between Solution-State Dynamics of an Individual Protein and the Sequence and Conformational Diversity of its Family

Released:
DOI: 10.2210/pdb2kn5/pdb
PDB entry 2kn5 coloured by chain, ensemble of 50 models, front view.
PDB entry 2kn5 coloured by chain, ensemble of 50 models, side view.
PDB entry 2kn5 coloured by chain, ensemble of 50 models, top view.
Source organism: Homo sapiens
Primary publication:
A correspondence between solution-state dynamics of an individual protein and the sequence and conformational diversity of its family.
Friedland GD, Lakomek NA, Griesinger C, Meiler J, Kortemme T
PLoS Comput Biol 5 e1000393 (2009)
PMID: 19478996

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143327 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin Chain: A
Molecule details ›
Chain: A
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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: Monte Carlo optimization of ensemble members
Expression system: Escherichia coli

Quick links

Citations

7 review citations

The interface of protein structure, protein biophysics, and molecular evolution.
Liberles et al. (2012)
6 more

3 mentions without citation

Protein structure validation and refinement using amide proton chemical shifts derived from quantum mechanics.
Christensen et al. (2013)
2 more