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Solution NMR

Solution NMR structure of a Thiamine Biosynthesis (ThiS) Protein RPA3574 from Rhodopseudomonas palustris refined with NH RDCs. Northeast Structural Genomics Consortium target RpR325

Released:
DOI: 10.2210/pdb2lek/pdb
PDB entry 2lek coloured by chain, ensemble of 20 models, front view.
PDB entry 2lek coloured by chain, ensemble of 20 models, side view.
PDB entry 2lek coloured by chain, ensemble of 20 models, top view.
Source organism: Rhodopseudomonas palustris
Entry authors: Ramelot TA, Cort JR, Lee H, Wang H, Ciccosanti C, Jiang M, Nair R, Rost B, Acton TB, Xiao R, Swapna G, Everett JK, Prestegard JH, Montelione GT, Kennedy MA, Northeast Structural Genomics Consortium (NESG)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179953 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sulfur carrier protein ThiS Chain: A
Molecule details ›
Chain: A
Length: 73 amino acids
Theoretical weight: 8.11 KDa
Source organism: Rhodopseudomonas palustris
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6N3W8 (Residues: 1-65; Coverage: 100%)
Gene names: RPA3574, TX73_018525, thiS
Sequence domains: ThiS family
Structure domains: Ubiquitin-like (UB roll)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 95%
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

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