› 1rfo

Solution NMR

Trimeric Foldon of the T4 phagehead fibritin

Released:
DOI: 10.2210/pdb1rfo/pdb
PDB entry 1rfo coloured by chain, ensemble of 10 models, front view.
PDB entry 1rfo coloured by chain, ensemble of 10 models, side view.
PDB entry 1rfo coloured by chain, ensemble of 10 models, top view.
Source organism: Escherichia virus T4
Primary publication:
Very fast folding and association of a trimerization domain from bacteriophage T4 fibritin.
Güthe S, Kapinos L, Möglich A, Meier S, Grzesiek S, Kiefhaber T
J Mol Biol 337 905-15 (2004)
PMID: 15033360

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145168 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fibritin Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 27 amino acids
Theoretical weight: 3.08 KDa
Source organism: Escherichia virus T4
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P10104 (Residues: 458-484; Coverage: 6%)
Gene name: wac

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing with torsion angle dynamics
Expression system: Escherichia coli BL21(DE3)

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Citations

7 review citations

Unusual biophysics of intrinsically disordered proteins.
Uversky VN. (2013)
6 more

16 mentions without citation

Hierarchical design of artificial proteins and complexes toward synthetic structural biology.
Arai R. (2018)
15 more