› 4hu7

X-ray diffraction
1.4Å resolution

E. coli thioredoxin variant with Pro76 as single proline residue

Released:
DOI: 10.2210/pdb4hu7/pdb
PDB entry 4hu7 coloured by chain, front view.
PDB entry 4hu7 coloured by chain, side view.
PDB entry 4hu7 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

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-141959 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioredoxin 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 108 amino acids
Theoretical weight: 11.58 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0AA25 (Residues: 2-109; Coverage: 99%)
Gene names: JW5856, b3781, fipA, trxA, tsnC
Sequence domains: Thioredoxin
Structure domains: Glutaredoxin

Ligands and Environments

2 bound ligands:
Ligand CU 2 x CU
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P21
Unit cell:
a: 33.85Å b: 60.88Å c: 45.33Å
α: 90° β: 100.38° γ: 90°
R-values:
R R work R free
0.163 0.162 0.198
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

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

2 mentions without citation

Acceleration of protein folding by four orders of magnitude through a single amino acid substitution.
Roderer et al. (2015)
1 more