› 2i1k

X-ray diffraction
3Å resolution

Moesin from Spodoptera frugiperda reveals the coiled-coil domain at 3.0 angstrom resolution

Released:
DOI: 10.2210/pdb2i1k/pdb
PDB entry 2i1k coloured by chain, front view.
PDB entry 2i1k coloured by chain, side view.
PDB entry 2i1k coloured by chain, top view.
Source organism: Spodoptera frugiperda
Primary publication:
Self-masking in an intact ERM-merlin protein: an active role for the central alpha-helical domain.
Li Q, Nance MR, Kulikauskas R, Nyberg K, Fehon R, Karplus PA, Bretscher A, Tesmer JJ
J Mol Biol 365 1446-59 (2007)
PMID: 17134719

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106512 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:

Ligands and Environments

3 bound ligands:
Ligand CL 1 x CL
Ligand URE 1 x URE
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: R32
Unit cell:
a: 126.94Å b: 126.94Å c: 272.517Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.184 0.181 0.249

Quick links

Citations

17 review citations

Organizing the cell cortex: the role of ERM proteins.
Fehon et al. (2010)
16 more

15 mentions without citation

Model membranes to shed light on the biochemical and physical properties of ezrin/radixin/moesin.
Maniti et al. (2013)
14 more