4tt1

X-ray diffraction
2.75Å resolution

Crystal structure of fragment 1600-1733 of HSV1 UL36, native

Released:

Function and Biology Details

Reaction catalysed:
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:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-145210 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Large tegument protein deneddylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 138 amino acids
Theoretical weight: 15.09 KDa
Source organism: Human alphaherpesvirus 1 strain 17
Expression system: Escherichia coli
UniProt:
  • Canonical: P10220 (Residues: 1625-1757; Coverage: 4%)
Gene name: UL36

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P6122
Unit cell:
a: 110.217Å b: 110.217Å c: 159.939Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.203 0.201 0.242
Expression system: Escherichia coli