› 4kln

X-ray diffraction
2.62Å resolution

Structure of p97 N-D1 A232E mutant in complex with ATPgS

Released:
DOI: 10.2210/pdb4kln/pdb
PDB entry 4kln coloured by chain, front view.
PDB entry 4kln coloured by chain, side view.
PDB entry 4kln coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Altered intersubunit communication is the molecular basis for functional defects of pathogenic p97 mutants.
Tang WK, Xia D
J Biol Chem 288 36624-35 (2013)
PMID: 24196964

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157184 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transitional endoplasmic reticulum ATPase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 489 amino acids
Theoretical weight: 54.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55072 (Residues: 1-481; Coverage: 60%)
Gene names: HEL-220, HEL-S-70, VCP
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand AGS 6 x AGS
Ligand MG 6 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P1
Unit cell:
a: 91.147Å b: 104.514Å c: 109.528Å
α: 98.11° β: 90.55° γ: 92.72°
R-values:
R R work R free
0.275 0.274 0.289
Expression system: Escherichia coli

Quick links

Citations

11 review citations

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

6 mentions without citation

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