› 2lys

Solution NMR

NOE-based 3D structure of the monomeric partially-folded intermediate of CylR2 at 257K (-16 Celsius degrees)

Released:
DOI: 10.2210/pdb2lys/pdb
PDB entry 2lys coloured by chain, ensemble of 20 models, front view.
PDB entry 2lys coloured by chain, ensemble of 20 models, side view.
PDB entry 2lys coloured by chain, ensemble of 20 models, top view.
Source organism: Enterococcus faecalis
Primary publication:
Cold denaturation of a protein dimer monitored at atomic resolution.
Jaremko M, Jaremko Ł, Kim HY, Cho MK, Schwieters CD, Giller K, Becker S, Zweckstetter M
Nat Chem Biol 9 264-70 (2013)
PMID: 23396077

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186599 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
HTH cro/C1-type domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 66 amino acids
Theoretical weight: 7.72 KDa
Source organism: Enterococcus faecalis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8VL32 (Residues: 1-66; Coverage: 100%)
Gene names: EU507_14965, cylR2
Sequence domains: Helix-turn-helix
Structure domains: lambda repressor-like DNA-binding domains

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 73%
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Water Determines the Structure and Dynamics of Proteins.
Bellissent-Funel et al. (2016)
1 more

9 mentions without citation

Functional and Regulatory Roles of Fold-Switching Proteins.
Kim et al. (2021)
8 more