› 1pwt

X-ray diffraction
1.77Å resolution

THERMODYNAMIC ANALYSIS OF ALPHA-SPECTRIN SH3 AND TWO OF ITS CIRCULAR PERMUTANTS WITH DIFFERENT LOOP LENGTHS: DISCERNING THE REASONS FOR RAPID FOLDING IN PROTEINS

Released:
DOI: 10.2210/pdb1pwt/pdb
PDB entry 1pwt coloured by chain, front view.
PDB entry 1pwt coloured by chain, side view.
PDB entry 1pwt coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Thermodynamic analysis of alpha-spectrin SH3 and two of its circular permutants with different loop lengths: discerning the reasons for rapid folding in proteins.
Martínez JC, Viguera AR, Berisio R, Wilmanns M, Mateo PL, Filimonov VV, Serrano L
Biochemistry 38 549-59 (1999)
PMID: 9888794

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: 61 amino acids
Theoretical weight: 7.04 KDa
Source organism: Gallus gallus
UniProt:
  • Canonical: P07751 (Residues: 967-1025; Coverage: 2%)
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
X-ray source: OTHER
Spacegroup: P212121
Unit cell:
a: 33Å b: 42.4Å c: 49.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.187 0.246

Quick links

Citations

4 review citations

Malleability of protein folding pathways: a simple reason for complex behaviour.
Lindberg et al. (2007)
3 more

1 mention without citation

Folding free energy function selects native-like protein sequences in the core but not on the surface.
Jaramillo et al. (2002)