› 6t3x

X-ray diffraction
1.48Å resolution

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147815 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nuclear egress protein 1; Nuclear egress protein 2 Chains: A, C
Molecule details ›
Chains: A, C
Length: 214 amino acids
Theoretical weight: 23.92 KDa
Source organism: Human herpesvirus 5 strain AD169
Expression system: Escherichia coli
UniProt:
  • Canonical: P16791 (Residues: 1-171; Coverage: 43%)
  • Canonical: P16794 (Residues: 59-87; Coverage: 8%)
Gene names: NEC1, NEC2, UL50, UL53
Sequence domains: Herpesvirus virion protein U34

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P21
Unit cell:
a: 37.27Å b: 82.57Å c: 63.66Å
α: 90° β: 95.097° γ: 90°
R-values:
R R work R free
0.194 0.192 0.225
Expression system: Escherichia coli

Quick links

Citations

6 review citations

The Cytomegalovirus Protein Kinase pUL97:Host Interactions, Regulatory Mechanisms and Antiviral Drug Targeting.
Steingruber et al. (2020)
5 more

1 mention without citation

High-resolution crystal structures of two prototypical β- and γ-herpesviral nuclear egress complexes unravel the determinants of subfamily specificity.
Muller et al. (2020)