Function and Biology Details
Biochemical function:
- not assigned
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169881 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Vacuolar protein sorting-associated protein VTA1
Molecule details ›
Chain: A
Length: 167 amino acids
Theoretical weight: 19.06 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
Sequence domains: Vta1 like
Structure domains: Vacuolar protein sorting-associated protein vta1
Length: 167 amino acids
Theoretical weight: 19.06 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
- Canonical:
Q06263 (Residues: 1-167; Coverage: 51%)
Sequence domains: Vta1 like
Structure domains: Vacuolar protein sorting-associated protein vta1
Vacuolar protein-sorting-associated protein 60
Molecule details ›
Chain: B
Length: 59 amino acids
Theoretical weight: 6.61 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
Sequence domains: Snf7
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Length: 59 amino acids
Theoretical weight: 6.61 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
- Canonical: Q03390 (Residues: 128-186; Coverage: 26%)
Sequence domains: Snf7
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
Chemical shift assignment:
92%
Refinement method:
simulated annealing
Expression system: Escherichia coli
