› 3qc8

X-ray diffraction
2.2Å resolution

Crystal Structure of FAF1 UBX Domain In Complex with p97/VCP N Domain Reveals The Conserved FcisP Touch-Turn Motif of UBX Domain Suffering Conformational Change

Released:
DOI: 10.2210/pdb3qc8/pdb
PDB entry 3qc8 coloured by chain, front view.
PDB entry 3qc8 coloured by chain, side view.
PDB entry 3qc8 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of FAF1 UBX domain in complex with p97/VCP N domain reveals a conformational change in the conserved FcisP touch-turn motif of UBX domain.
Kim KH, Kang W, Suh SW, Yang JK
Proteins 79 2583-7 (2011)
PMID: 21739474

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
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: 178 amino acids
Theoretical weight: 20.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55072 (Residues: 21-196; Coverage: 22%)
Gene names: HEL-220, HEL-S-70, VCP
Sequence domains:
Structure domains:
FAS-associated factor 1 Chain: B
Molecule details ›
Chain: B
Length: 84 amino acids
Theoretical weight: 9.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UNN5 (Residues: 571-650; Coverage: 12%)
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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 4A
Spacegroup: C2221
Unit cell:
a: 58.07Å b: 72.74Å c: 130.59Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.216 0.25
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Control of p97 function by cofactor binding.
Buchberger et al. (2015)
5 more

3 mentions without citation

Structure and function of the AAA+ ATPase p97/Cdc48p.
Xia et al. (2016)
2 more