› 6t00

X-ray diffraction
2.1Å resolution

Crystal structure of Cold Shock Protein B (CSP-B) containing 4-F-Phe modified residues

Released:
DOI: 10.2210/pdb6t00/pdb
PDB entry 6t00 coloured by chain, front view.
PDB entry 6t00 coloured by chain, side view.
PDB entry 6t00 coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
What does fluorine do to a protein? Thermodynamic, and highly-resolved structural insights into fluorine-labelled variants of the cold shock protein.
Welte H, Zhou T, Mihajlenko X, Mayans O, Kovermann M
Sci Rep 10 2640 (2020)
PMID: 32060391

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152196 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cold shock protein CspB Chain: A
Molecule details ›
Chain: A
Length: 66 amino acids
Theoretical weight: 7.43 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P32081 (Residues: 1-66; Coverage: 99%)
Gene names: BSU09100, cspA, cspB
Sequence domains: 'Cold-shock' DNA-binding domain

Ligands and Environments

2 bound ligands:
Ligand NHE 1 x NHE
Ligand GOL 1 x GOL
1 modified residue:
Ligand PFF 7 x PFF

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P43212
Unit cell:
a: 54.94Å b: 54.94Å c: 57.71Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.199 0.252
Expression system: Escherichia coli

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Citations

5 review citations

Small, but powerful and attractive: 19F in biomolecular NMR.
Gronenborn AM. (2022)
4 more