› 3fhk

X-ray diffraction
2.3Å resolution

Crystal structure of APC1446, B.subtilis YphP disulfide isomerase

Released:
DOI: 10.2210/pdb3fhk/pdb
PDB entry 3fhk coloured by chain, front view.
PDB entry 3fhk coloured by chain, side view.
PDB entry 3fhk coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Structure and function of Bacillus subtilis YphP, a prokaryotic disulfide isomerase with a CXC catalytic motif .
Derewenda U, Boczek T, Gorres KL, Yu M, Hung LW, Cooper D, Joachimiak A, Raines RT, Derewenda ZS
Biochemistry 48 8664-71 (2009)
PMID: 19653655

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
homo trimer
Assembly name:
PDBe Complex ID:
PDB-CPX-156953 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bacilliredoxin BrxA Chains: A, D, E, F
Molecule details ›
Chains: A, D, E, F
Length: 147 amino acids
Theoretical weight: 16.05 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P54170 (Residues: 1-144; Coverage: 100%)
Gene names: BSU21860, brxA, yphP
Sequence domains: Disulphide isomerase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 12 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P41212
Unit cell:
a: 68.161Å b: 68.161Å c: 302.024Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.19 0.246
Expression system: Escherichia coli

Quick links

Citations

8 review citations

How proteins form disulfide bonds.
Depuydt et al. (2011)
7 more

3 mentions without citation

Redox regulation by reversible protein S-thiolation in Gram-positive bacteria.
Imber et al. (2019)
2 more