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X-ray diffraction
2.1Å resolution

Crystal structure of the ankyrin-binding domain of human erythroid spectrin

Released:
DOI: 10.2210/pdb3edu/pdb
PDB entry 3edu coloured by chain, front view.
PDB entry 3edu coloured by chain, side view.
PDB entry 3edu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The structure of the ankyrin-binding site of beta-spectrin reveals how tandem spectrin-repeats generate unique ligand-binding properties.
Stabach PR, Simonović I, Ranieri MA, Aboodi MS, Steitz TA, Simonović M, Morrow JS
Blood 113 5377-84 (2009)
PMID: 19168783

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-145745 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Spectrin beta chain, erythrocytic Chain: A
Molecule details ›
Chain: A
Length: 218 amino acids
Theoretical weight: 24.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11277 (Residues: 1692-1907; Coverage: 10%)
Gene names: SPTB, SPTB1
Sequence domains: Spectrin repeat
Structure domains: Methane Monooxygenase Hydroxylase; Chain G, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: F222
Unit cell:
a: 74.823Å b: 111.746Å c: 127.734Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.21 0.252
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Membrane domains based on ankyrin and spectrin associated with cell-cell interactions.
Bennett et al. (2009)
9 more

6 mentions without citation

The structure of the ankyrin-binding site of beta-spectrin reveals how tandem spectrin-repeats generate unique ligand-binding properties.
Stabach et al. (2009)
5 more