5ifs

X-ray diffraction
2.46Å resolution

Quantitative interaction mapping reveals an extended ubiquitin regulatory domain in ASPL that disrupts functional p97 hexamers and induces cell death

Released:

Function and Biology Details

Reaction catalysed:
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-157180 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tether containing UBX domain for GLUT4 Chains: A, C
Molecule details ›
Chains: A, C
Length: 237 amino acids
Theoretical weight: 26.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9BZE9 (Residues: 317-553; Coverage: 43%)
Gene names: ASPL, ASPSCR1, RCC17, TUG, UBXD9, UBXN9
Sequence domains: UBX domain
Transitional endoplasmic reticulum ATPase Chains: B, D
Molecule details ›
Chains: B, D
Length: 481 amino acids
Theoretical weight: 53.51 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P55072 (Residues: 1-481; Coverage: 60%)
Gene names: HEL-220, HEL-S-70, VCP
Sequence domains:
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P21
Unit cell:
a: 69.844Å b: 132.914Å c: 96.121Å
α: 90° β: 110.15° γ: 90°
R-values:
R R work R free
0.204 0.201 0.251
Expression system: Escherichia coli BL21(DE3)