› 6fls

X-ray diffraction
2.8Å resolution

Pentapeptide repeat family protein from Clostridium botulinum

Released:
DOI: 10.2210/pdb6fls/pdb
PDB entry 6fls coloured by chain, front view.
PDB entry 6fls coloured by chain, side view.
PDB entry 6fls coloured by chain, top view.
Source organism: Clostridium botulinum
Primary publication:
Cotranslational Folding of a Pentarepeat β-Helix Protein.
Notari L, Martínez-Carranza M, Farías-Rico JA, Stenmark P, von Heijne G
J Mol Biol 430 5196-5206 (2018)
PMID: 30539762

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-166721 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pentapeptide repeat family protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 239 amino acids
Theoretical weight: 27.37 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli

Ligands and Environments

1 bound ligand:
Ligand GOL 15 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P21
Unit cell:
a: 107.751Å b: 108.475Å c: 112.89Å
α: 90° β: 94.6° γ: 90°
R-values:
R R work R free
0.172 0.17 0.205
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Cotranslational Folding of Proteins on the Ribosome.
Liutkute et al. (2020)
1 more

1 mention without citation

Type I beta turns make a new twist in pentapeptide repeat proteins: Crystal structure of Alr5209 from Nostoc sp. PCC 7120 determined at 1.7 angström resolution.
Zhang et al. (2019)