› 1tud

X-ray diffraction
1.77Å resolution

ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, CIRCULAR PERMUTANT, CUT AT N47-D48

Released:
DOI: 10.2210/pdb1tud/pdb
PDB entry 1tud coloured by chain, front view.
PDB entry 1tud coloured by chain, side view.
PDB entry 1tud coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics.
Viguera AR, Blanco FJ, Serrano L
J Mol Biol 247 670-81 (1995)
PMID: 7723022

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139741 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Spectrin alpha chain, non-erythrocytic 1 Chain: A
Molecule details ›
Chain: A
Length: 62 amino acids
Theoretical weight: 7.13 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli
UniProt:
  • Canonical: P07751 (Residues: 949-1010; Coverage: 3%)
Gene names: SPTA2, SPTAN1
Sequence domains: SH3 domain
Structure domains: SH3 Domains

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 31.95Å b: 42.88Å c: 54.19Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.184 0.248
Expression system: Escherichia coli

Quick links

Citations

10 review citations

How do small single-domain proteins fold?
Jackson SE. (1998)
9 more

4 mentions without citation

Protein reconstitution and three-dimensional domain swapping: benefits and constraints of covalency.
Carey et al. (2007)
3 more