Function and Biology Details
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143467 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
EH domain-containing and endocytosis protein 1
Molecule details ›
Chain: A
Length: 43 amino acids
Theoretical weight: 4.69 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: UBA/TS-N domain
Structure domains: DNA helicase RuvA subunit, C-terminal domain
Length: 43 amino acids
Theoretical weight: 4.69 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
P34216 (Residues: 1339-1381; Coverage: 3%)
Sequence domains: UBA/TS-N domain
Structure domains: DNA helicase RuvA subunit, C-terminal domain
Ubiquitin
Molecule details ›
Chain: B
Length: 76 amino acids
Theoretical weight: 8.57 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Length: 76 amino acids
Theoretical weight: 8.57 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21
UniProt:
- Canonical: P0CG63 (Residues: 305-380; Coverage: 20%)
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Refinement method:
Torsion angle dynamics and simulated annealing
Expression system: Escherichia coli BL21
