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Solution NMR

Solution NMR Structure of Protein YKR049C from Saccharomyces cerevisiae. Ontario Centre for Structural Proteomics target YST0250_1_133; Northeast Structural Genomics Consortium YTYst250

Released:
DOI: 10.2210/pdb1wpi/pdb
PDB entry 1wpi coloured by chain, ensemble of 20 models, front view.
PDB entry 1wpi coloured by chain, ensemble of 20 models, side view.
PDB entry 1wpi coloured by chain, ensemble of 20 models, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Solution structure of YKR049C, a putative redox protein from Saccharomyces cerevisiae.
Jung JW, Yee A, Wu B, Arrowsmith CH, Lee W
J Biochem Mol Biol 38 550-4 (2005)
PMID: 16202234

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153132 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative redox protein FMP46, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 133 amino acids
Theoretical weight: 15.67 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P36141 (Residues: 1-133; Coverage: 100%)
Gene names: FMP46, YKR049C
Sequence domains: Protein of unknown function (DUF1687)
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics/CANDID method
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Structural proteomics by NMR spectroscopy.
Shin et al. (2008)
12 other articles

2 mentions without citation

Evolution of domain-peptide interactions to coadapt specificity and affinity to functional diversity.
Kelil et al. (2016)
1 more