› 1bb1

X-ray diffraction
1.8Å resolution

CRYSTAL STRUCTURE OF A DESIGNED, THERMOSTABLE HETEROTRIMERIC COILED COIL

Released:
DOI: 10.2210/pdb1bb1/pdb
PDB entry 1bb1 coloured by chain, front view.
PDB entry 1bb1 coloured by chain, side view.
PDB entry 1bb1 coloured by chain, top view.
Source organism: synthetic construct
Primary publication:
Crystal structure of a designed, thermostable, heterotrimeric coiled coil.
Nautiyal S, Alber T
Protein Sci 8 84-90 (1999)
PMID: 10210186

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162114 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
DESIGNED, THERMOSTABLE HETEROTRIMERIC COILED COIL Chain: A
Molecule details ›
Chain: A
Length: 36 amino acids
Theoretical weight: 3.7 KDa
Source organism: synthetic construct
Expression system: Not provided
DESIGNED, THERMOSTABLE HETEROTRIMERIC COILED COIL Chain: B
Molecule details ›
Chain: B
Length: 36 amino acids
Theoretical weight: 3.84 KDa
Source organism: synthetic construct
Expression system: Not provided
DESIGNED, THERMOSTABLE HETEROTRIMERIC COILED COIL Chain: C
Molecule details ›
Chain: C
Length: 36 amino acids
Theoretical weight: 3.67 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P21
Unit cell:
a: 21.93Å b: 35.01Å c: 66.46Å
α: 90° β: 93.7° γ: 90°
R-values:
R R work R free
0.208 0.208 0.269
Expression system: Not provided

Quick links

Citations

3 review citations

Fifty years of coiled-coils and alpha-helical bundles: a close relationship between sequence and structure.
Parry et al. (2008)
2 more

3 mentions without citation

A novel cell binding site in the coiled-coil domain of laminin involved in capillary morphogenesis.
Sanz et al. (2003)
2 more