3ggz

X-ray diffraction
3.8Å resolution

Crystal Structure of S.cerevisiae Ist1 N-terminal domain in complex with Did2 MIM motif

Released:

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-156885 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Vacuolar protein sorting-associated protein IST1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 193 amino acids
Theoretical weight: 22.38 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P53843 (Residues: 1-193; Coverage: 65%)
Gene names: IST1, N0809, YNL265C
Sequence domains: Regulator of Vps4 activity in the MVB pathway
Structure domains: Vacuolar protein sorting-associated protein Ist1
Vacuolar protein-sorting-associated protein 46 Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 29 amino acids
Theoretical weight: 3.34 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P69771 (Residues: 176-204; Coverage: 14%)
Gene names: CHM1, DID2, FTI1, VPS46, YKR035W-A

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P4222
Unit cell:
a: 165.916Å b: 165.916Å c: 121.559Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.289 0.289 0.307
Expression system: Escherichia coli