- PDB-1pqs: Solution structure of the C-terminal OPCA domain of yCdc24p -
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Open data
ID or keywords:
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Basic information
Entry
Database: PDB / ID: 1pqs
Title
Solution structure of the C-terminal OPCA domain of yCdc24p
Components
Cell division control protein 24
Keywords
CELL CYCLE / Alpha and Beta protein
Function / homology
Function and homology information
regulation of pheromone-dependent signal transduction involved in conjugation with cellular fusion / chemotropism / Cdc24p-Far1p-Gbetagamma complex / septin ring organization / protein localization to cell cortex / division septum / PAR polarity complex / cellular bud site selection / incipient cellular bud site / cellular bud tip ...regulation of pheromone-dependent signal transduction involved in conjugation with cellular fusion / chemotropism / Cdc24p-Far1p-Gbetagamma complex / septin ring organization / protein localization to cell cortex / division septum / PAR polarity complex / cellular bud site selection / incipient cellular bud site / cellular bud tip / regulation of exit from mitosis / cellular bud neck / mating projection tip / regulation of Rho protein signal transduction / establishment of cell polarity / guanyl-nucleotide exchange factor activity / cell cortex / intracellular signal transduction / nucleus / cytoplasm Similarity search - Function
Mass: 8973.029 Da / Num. of mol.: 1 / Fragment: C-terminal OPCA domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Gene: Cdc24p / Plasmid: pet17b / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P11433
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Type
1
1
1
4D 15N-separated NOESY
1
2
1
4D 13C/15N-separated NOESY
1
3
1
3D 13C-separated NOESY
2
4
2
3D 15N-separated NOESY
NMR details
Text: the structures are based on a total of 1754 restraints, 1615 are NOE-derived distance constraints, 75 dihedral angle restraints, 64 distance restraints from hydrogen bonds.
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