5kiw

X-ray diffraction
3.41Å resolution

p97 ND1-L198W in complex with VIMP

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis for nucleotide-modulated p97 association with the ER membrane.
OpenAccess logo Cell Discov 3 17045 (2017)
PMID: 29238611

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Transitional endoplasmic reticulum ATPase Chains: A, B
Molecule details ›
Chains: A, B
Length: 468 amino acids
Theoretical weight: 52.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P55072 (Residues: 1-460; Coverage: 57%)
Gene name: VCP
Sequence domains:
Selenoprotein S Chains: C, D
Molecule details ›
Chains: C, D
Length: 81 amino acids
Theoretical weight: 9.73 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9BQE4 (Residues: 42-42, 49-122; Coverage: 40%)
Gene names: AD-015, SBBI8, SELENOS, SELS, VIMP

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P622
Unit cell:
a: 153.772Å b: 153.772Å c: 240.641Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.236 0.233 0.294
Expression system: Escherichia coli BL21(DE3)