› 1ni2

X-ray diffraction
2.3Å resolution

Structure of the active FERM domain of Ezrin

Released:
DOI: 10.2210/pdb1ni2/pdb
PDB entry 1ni2 coloured by chain, front view.
PDB entry 1ni2 coloured by chain, side view.
PDB entry 1ni2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the active N-terminal domain of Ezrin. Conformational and mobility changes identify keystone interactions.
Smith WJ, Nassar N, Bretscher A, Cerione RA, Karplus PA
J Biol Chem 278 4949-56 (2003)
PMID: 12429733

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147312 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ezrin Chains: A, B
Molecule details ›
Chains: A, B
Length: 296 amino acids
Theoretical weight: 34.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P15311 (Residues: 2-297; Coverage: 51%)
Gene names: EZR, VIL2
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P21
Unit cell:
a: 48.489Å b: 112.802Å c: 66.301Å
α: 90° β: 102.32° γ: 90°
R-values:
R R work R free
0.231 0.23 0.283
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

21 review citations

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

13 mentions without citation

Integrating 3D structural information into systems biology.
Murray et al. (2021)
12 more