3kbt

X-ray diffraction
2.75Å resolution

Crystal structure of the ankyrin binding domain of human erythroid beta spectrin (repeats 13-15) in complex with the spectrin binding domain of human erythroid ankyrin (ZU5-ANK)

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis for spectrin recognition by ankyrin.
Blood 115 4093-101 (2010)
PMID: 20101027

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-145746 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Spectrin beta chain, erythrocytic Chains: A, B
Molecule details ›
Chains: A, B
Length: 326 amino acids
Theoretical weight: 37.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11277 (Residues: 1583-1906; Coverage: 15%)
Gene names: SPTB, SPTB1
Sequence domains: Spectrin repeat
Structure domains: Methane Monooxygenase Hydroxylase; Chain G, domain 1
Ankyrin-1 Chains: C, D
Molecule details ›
Chains: C, D
Length: 161 amino acids
Theoretical weight: 17.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P16157 (Residues: 911-1068; Coverage: 8%)
Gene names: ANK, ANK1
Sequence domains: ZU5 domain
Structure domains: Chondroitinase Ac; Chain A, domain 3

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: P212121
Unit cell:
a: 90.45Å b: 95.66Å c: 137.93Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.247 0.245 0.292
Expression system: Escherichia coli