› 6uhw

Solution NMR

Solution structure of an organic hydroperoxide resistance protein from Burkholderia pseudomallei. Seattle Structural Genomics Center for Infectious Disease target BupsA.00074.a.

Released:
DOI: 10.2210/pdb6uhw/pdb
PDB entry 6uhw coloured by chain, ensemble of 20 models, front view.
PDB entry 6uhw coloured by chain, ensemble of 20 models, side view.
PDB entry 6uhw coloured by chain, ensemble of 20 models, top view.
Source organism: Burkholderia pseudomallei 1710b
Primary publication:
Backbone and side chain (1)H, (13)C, and (15)N NMR assignments for the organic hydroperoxide resistance protein (Ohr) from Burkholderia pseudomallei.
Buchko GW, Hewitt SN, Napuli AJ, Van Voorhis WC, Myler PJ
Biomol NMR Assign 3 163-6 (2009)
PMID: 19888681

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174639 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Organic hydroperoxide resistance protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 139 amino acids
Theoretical weight: 14.41 KDa
Source organism: Burkholderia pseudomallei 1710b
Expression system: Escherichia coli
UniProt:
  • Canonical: Q3JK82 (Residues: 1-139; Coverage: 100%)
Gene names: BURPS1710b_A0863, ohr
Sequence domains: OsmC-like protein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 40%
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Cytosolic expression, solution structures, and molecular dynamics simulation of genetically encodable disulfide-rich de novo designed peptides.
Buchko et al. (2018)