› 2kox

Solution NMR

NMR residual dipolar couplings identify long range correlated motions in the backbone of the protein ubiquitin

Released:
DOI: 10.2210/pdb2kox/pdb
PDB entry 2kox coloured by chain, ensemble of 640 models, front view.
PDB entry 2kox coloured by chain, ensemble of 640 models, side view.
PDB entry 2kox coloured by chain, ensemble of 640 models, top view.
Source organism: Homo sapiens
Primary publication:
Weak long-range correlated motions in a surface patch of ubiquitin involved in molecular recognition.
Fenwick RB, Esteban-Martín S, Richter B, Lee D, Walter KF, Milovanovic D, Becker S, Lakomek NA, Griesinger C, Salvatella X
J Am Chem Soc 133 10336-9 (2011)
PMID: 21634390

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-158832 (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: P62987 (Residues: 1-76; Coverage: 59%)
Gene names: UBA52, UBCEP2
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: simulated annealing, molecular dynamics
Expression system: Escherichia coli

Quick links

Citations

15 review citations

Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell.
Wei et al. (2016)
14 more

12 mentions without citation

NMR studies of dynamic biomolecular conformational ensembles.
Torchia DA. (2015)
11 more