› 2m6n

Solution NMR

3D solution structure of EMI1 (Early Mitotic Inhibitor 1)

Released:
DOI: 10.2210/pdb2m6n/pdb
PDB entry 2m6n coloured by chain, ensemble of 20 models, front view.
PDB entry 2m6n coloured by chain, ensemble of 20 models, side view.
PDB entry 2m6n coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Electron microscopy structure of human APC/C(CDH1)-EMI1 reveals multimodal mechanism of E3 ligase shutdown.
Frye JJ, Brown NG, Petzold G, Watson ER, Grace CR, Nourse A, Jarvis MA, Kriwacki RW, Peters JM, Stark H, Schulman BA
Nat Struct Mol Biol 20 827-35 (2013)
PMID: 23708605

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193859 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
F-box only protein 5 Chain: A
Molecule details ›
Chain: A
Length: 86 amino acids
Theoretical weight: 9.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UKT4 (Residues: 364-447; Coverage: 19%)
Gene names: EMI1, FBX5, FBXO5
Structure domains: N-terminal domain of TfIIb

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 89%
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

22 review citations

Intrinsically disordered proteins and intrinsically disordered protein regions.
Oldfield et al. (2014)
21 more

3 mentions without citation

Atomic structure of the APC/C and its mechanism of protein ubiquitination.
Chang et al. (2015)
2 more