4kdi

X-ray diffraction
1.86Å resolution

Crystal structure of p97/VCP N in complex with OTU1 UBXL

Released:

Function and Biology Details

Reactions catalysed:
ATP + H(2)O = ADP + phosphate
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-155089 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Transitional endoplasmic reticulum ATPase Chains: A, B
Molecule details ›
Chains: A, B
Length: 193 amino acids
Theoretical weight: 21.81 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:
Ubiquitin thioesterase OTU1 Chains: C, D
Molecule details ›
Chains: C, D
Length: 90 amino acids
Theoretical weight: 9.69 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P43558 (Residues: 1-73; Coverage: 24%)
Gene names: OTU1, YFL044C
Sequence domains: OTU1, UBXL 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: P212121
Unit cell:
a: 42.819Å b: 88.609Å c: 143.535Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.214 0.257
Expression system: Escherichia coli