3qq8

X-ray diffraction
2Å resolution

Crystal structure of p97-N in complex with FAF1-UBX

Released:
Source organism: Homo sapiens
Primary publication:
Hierarchical binding of cofactors to the AAA ATPase p97.
Structure 19 833-43 (2011)
PMID: 21645854

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-157177 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Transitional endoplasmic reticulum ATPase Chain: A
Molecule details ›
Chain: A
Length: 186 amino acids
Theoretical weight: 20.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55072 (Residues: 2-187; Coverage: 23%)
Gene names: HEL-220, HEL-S-70, VCP
Sequence domains:
Structure domains:
FAS-associated factor 1 Chain: B
Molecule details ›
Chain: B
Length: 85 amino acids
Theoretical weight: 9.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UNN5 (Residues: 568-650; Coverage: 13%)
Gene names: CGI-03, FAF1, UBXD12, UBXN3A
Sequence domains: UBX domain
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P65
Unit cell:
a: 88.08Å b: 88.08Å c: 66.91Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.169 0.166 0.21
Expression system: Escherichia coli