Function and Biology Details
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171298 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin-like protein MDY2
Molecule details ›
Chain: A
Length: 81 amino acids
Theoretical weight: 9.17 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Length: 81 amino acids
Theoretical weight: 9.17 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
- Canonical:
Q12285 (Residues: 74-151; Coverage: 37%)
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Small glutamine-rich tetratricopeptide repeat-containing protein 2
Molecule details ›
Chains: B, C
Length: 74 amino acids
Theoretical weight: 7.89 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
Sequence domains: Homodimerisation domain of SGTA
Structure domains: Immunoglobulin FC, subunit C
Length: 74 amino acids
Theoretical weight: 7.89 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
- Canonical: Q12118 (Residues: 2-72; Coverage: 21%)
Sequence domains: Homodimerisation domain of SGTA
Structure domains: Immunoglobulin FC, subunit C
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Chemical shift assignment:
60%
Refinement method:
simulated annealing, experimentally driven docking
Expression system: Escherichia coli
