Function and Biology Details
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domain:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150415 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
mRNA 3'-end-processing protein RNA15
Molecule details ›
Chain: A
Length: 109 amino acids
Theoretical weight: 12.05 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
Structure domains: Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Length: 109 amino acids
Theoretical weight: 12.05 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
- Canonical:
P25299 (Residues: 127-232; Coverage: 36%)
Structure domains: Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
mRNA 3'-end-processing protein RNA14
Molecule details ›
Chain: B
Length: 53 amino acids
Theoretical weight: 6.05 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Length: 53 amino acids
Theoretical weight: 6.05 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
- Canonical: P25298 (Residues: 625-677; Coverage: 8%)
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
wwPDB Validation report is not available for this NMR entry.
Chemical shift assignment:
96%
Refinement method:
DGSA-distance geometry simulated annealing
Expression system: Escherichia coli
