› 1pra

Solution NMR

DETERMINATION OF THE NUCLEAR MAGNETIC RESONANCE SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN (RESIDUES 1 TO 69) OF THE 434 REPRESSOR AND COMPARISON WITH THE X-RAY CRYSTAL STRUCTURE

Released:
DOI: 10.2210/pdb1pra/pdb
PDB entry 1pra coloured by chain, ensemble of 20 models, front view.
PDB entry 1pra coloured by chain, ensemble of 20 models, side view.
PDB entry 1pra coloured by chain, ensemble of 20 models, top view.
Source organism: Phage 434
Primary publication:
Determination of the nuclear magnetic resonance solution structure of the DNA-binding domain (residues 1 to 69) of the 434 repressor and comparison with the X-ray crystal structure.
Neri D, Billeter M, Wüthrich K
J Mol Biol 223 743-67 (1992)
PMID: 1311771

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147628 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Repressor protein CI Chain: A
Molecule details ›
Chain: A
Length: 69 amino acids
Theoretical weight: 7.56 KDa
Source organism: Phage 434
Expression system: Not provided
UniProt:
  • Canonical: P16117 (Residues: 2-70; Coverage: 73%)
Gene name: CI
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
Expression system: Not provided

Quick links

Citations

2 review citations

Comparison of protein structures determined by NMR in solution and by X-ray diffraction in single crystals.
Billeter M. (1992)
1 more

3 mentions without citation

Host defense peptides in skin secretions of the Oregon spotted frog Rana pretiosa: implications for species resistance to chytridiomycosis.
Conlon et al. (2011)
2 more