› 4hua

X-ray diffraction
1.1Å resolution

E. coli thioredoxin variant with (4R)-FluoroPro76 as single proline residue

Released:
DOI: 10.2210/pdb4hua/pdb
PDB entry 4hua coloured by chain, front view.
PDB entry 4hua coloured by chain, side view.
PDB entry 4hua coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
(4R)- and (4S)-fluoroproline in the conserved cis-prolyl peptide bond of the thioredoxin fold: tertiary structure context dictates ring puckering.
Rubini M, Schärer MA, Capitani G, Glockshuber R
Chembiochem 14 1053-7 (2013)
PMID: 23712956

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-141959 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioredoxin 1 Chain: A
Molecule details ›
Chain: A
Length: 108 amino acids
Theoretical weight: 11.6 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AA25 (Residues: 2-109; Coverage: 99%)
Gene names: JW5856, b3781, fipA, trxA, tsnC
Sequence domains: Thioredoxin
Structure domains: Glutaredoxin

Ligands and Environments

1 bound ligand:
Ligand CU 1 x CU
1 modified residue:
Ligand FP9 1 x FP9

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: C2
Unit cell:
a: 88.36Å b: 48.69Å c: 31.49Å
α: 90° β: 101.98° γ: 90°
R-values:
R R work R free
0.16 0.159 0.172
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Fluoro amino acids: a rarity in nature, yet a prospect for protein engineering.
Odar et al. (2015)
4 more

3 mentions without citation

Biochemistry of fluoroprolines: the prospect of making fluorine a bioelement.
Kubyshkin et al. (2021)
2 more