› 3qca

X-ray diffraction
2.9Å 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/pdb3qca/pdb
PDB entry 3qca coloured by chain, front view.
PDB entry 3qca coloured by chain, side view.
PDB entry 3qca coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human FAF1 UBX domain reveals a novel FcisP touch-turn motif in p97/VCP-binding region.
Kang W, Yang JK
Biochem Biophys Res Commun 407 531-4 (2011)
PMID: 21414298

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193999 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FAS-associated factor 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
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: F23
Unit cell:
a: 175.73Å b: 175.73Å c: 175.73Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.249 0.247 0.293
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

1 mention without citation

Crystallization and preliminary X-ray crystallographic analysis of the hexameric human p97/VCP ND1 fragment in complex with the UBX domain of human FAF1.
Kang et al. (2011)