› 2m0x

Solution NMR

Solution structure of U14Ub1, an engineered ubiquitin variant with increased affinity for USP14

Released:
DOI: 10.2210/pdb2m0x/pdb
PDB entry 2m0x coloured by chain, ensemble of 10 models, front view.
PDB entry 2m0x coloured by chain, ensemble of 10 models, side view.
PDB entry 2m0x coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Conformational dynamics control ubiquitin-deubiquitinase interactions and influence in vivo signaling.
Phillips AH, Zhang Y, Cunningham CN, Zhou L, Forrest WF, Liu PS, Steffek M, Lee J, Tam C, Helgason E, Murray JM, Kirkpatrick DS, Fairbrother WJ, Corn JE
Proc Natl Acad Sci U S A 110 11379-84 (2013)
PMID: 23801757

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-162947 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
engineered ubiquitin variant Chain: A
Molecule details ›
Chain: A
Length: 78 amino acids
Theoretical weight: 8.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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
Chemical shift assignment: 88%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Substrate specificity of the ubiquitin and Ubl proteases.
Ronau et al. (2016)
11 more

1 mention without citation

Conformational dynamics control ubiquitin-deubiquitinase interactions and influence in vivo signaling.
Phillips et al. (2013)