› 2o85

X-ray diffraction
2.2Å resolution

S. Aureus thioredoxin P31T mutant

Released:
DOI: 10.2210/pdb2o85/pdb
PDB entry 2o85 coloured by chain, front view.
PDB entry 2o85 coloured by chain, side view.
PDB entry 2o85 coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
The conserved active site proline determines the reducing power of Staphylococcus aureus thioredoxin.
Roos G, Garcia-Pino A, Van Belle K, Brosens E, Wahni K, Vandenbussche G, Wyns L, Loris R, Messens J
J Mol Biol 368 800-11 (2007)
PMID: 17368484

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-140938 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioredoxin Chain: A
Molecule details ›
Chain: A
Length: 107 amino acids
Theoretical weight: 11.74 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0A0K6 (Residues: 1-104; Coverage: 100%)
Gene name: trxA
Sequence domains: Thioredoxin
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P212121
Unit cell:
a: 41.717Å b: 49.452Å c: 54.473Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.196 0.245
Expression system: Escherichia coli BL21

Quick links

Citations

10 review citations

Structure, function, and mechanism of thioredoxin proteins.
Collet et al. (2010)
9 more

1 mention without citation

n→π* Interactions Modulate the Properties of Cysteine Residues and Disulfide Bonds in Proteins.
Kilgore et al. (2018)