› 5c1a

X-ray diffraction
3.8Å resolution

p97-N750D/R753D/M757D/Q760D in complex with ATP-gamma-S

Released:
DOI: 10.2210/pdb5c1a/pdb
PDB entry 5c1a coloured by chain, front view.
PDB entry 5c1a coloured by chain, side view.
PDB entry 5c1a coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural Basis of ATP Hydrolysis and Intersubunit Signaling in the AAA+ ATPase p97.
Hänzelmann P, Schindelin H
Structure 24 127-139 (2016)
PMID: 26712278

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
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, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 805 amino acids
Theoretical weight: 89.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P55072 (Residues: 2-806; Coverage: 100%)
Gene names: HEL-220, HEL-S-70, VCP
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand AGS 24 x AGS
Ligand MG 24 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P21
Unit cell:
a: 182.669Å b: 145.47Å c: 251.397Å
α: 90° β: 109.77° γ: 90°
R-values:
R R work R free
0.194 0.19 0.254
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

14 review citations

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

6 mentions without citation

Chaperoning Endoplasmic Reticulum-Associated Degradation (ERAD) and Protein Conformational Diseases.
Needham et al. (2019)
5 more