› 2l9v

Solution NMR

NMR structure of the FF domain L24A mutant's folding transition state

Released:
DOI: 10.2210/pdb2l9v/pdb
PDB entry 2l9v coloured by chain, ensemble of 9 models, front view.
PDB entry 2l9v coloured by chain, ensemble of 9 models, side view.
PDB entry 2l9v coloured by chain, ensemble of 9 models, top view.
Source organism: Homo sapiens
Primary publication:
Nonnative interactions in the FF domain folding pathway from an atomic resolution structure of a sparsely populated intermediate: an NMR relaxation dispersion study.
Korzhnev DM, Vernon RM, Religa TL, Hansen AL, Baker D, Fersht AR, Kay LE
J. Am. Chem. Soc. 133 10974-82 (2011)
PMID: 21639149

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130950 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pre-mRNA-processing factor 40 homolog A Chain: A
Molecule details ›
Chain: A
Length: 70 amino acids
Theoretical weight: 8.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O75400 (Residues: 381-450; Coverage: 7%)
Gene names: FBP11, FLAF1, FNBP3, HIP10, HSPC225, HYPA, PRPF40A
Sequence domains: FF domain
Structure domains: FF domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 34%
Refinement method: Monte Carlo
Expression system: Escherichia coli

Quick links

Citations

5 review citations

The how's and why's of protein folding intermediates.
Tsytlonok et al. (2013)
4 more

3 mentions without citation

NMR paves the way for atomic level descriptions of sparsely populated, transiently formed biomolecular conformers.
Sekhar et al. (2013)
2 more