3lbx

X-ray diffraction
2.8Å resolution

Crystal Structure of the Erythrocyte Spectrin Tetramerization Domain Complex

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Spectrin alpha chain, erythrocytic 1 Chain: A
Molecule details ›
Chain: A
Length: 161 amino acids
Theoretical weight: 18.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P02549 (Residues: 1-158; Coverage: 7%)
Gene names: SPTA, SPTA1
Sequence domains: Spectrin repeat
Structure domains: Methane Monooxygenase Hydroxylase; Chain G, domain 1
Spectrin beta chain, erythrocytic Chain: B
Molecule details ›
Chain: B
Length: 185 amino acids
Theoretical weight: 21.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11277 (Residues: 1902-2084; Coverage: 9%)
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 21-ID-F
Spacegroup: I41
Unit cell:
a: 213.901Å b: 213.901Å c: 31.461Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.269 0.268 0.299
Expression system: Escherichia coli