› 5doe

X-ray diffraction
3Å resolution

Crystal structure of the Human Cytomegalovirus UL53 (residues 72-292)

Released:
DOI: 10.2210/pdb5doe/pdb
PDB entry 5doe coloured by chain, front view.
PDB entry 5doe coloured by chain, side view.
PDB entry 5doe coloured by chain, top view.
Source organism: Human herpesvirus 5 strain AD169
Primary publication:
Unexpected features and mechanism of heterodimer formation of a herpesvirus nuclear egress complex.
Lye MF, Sharma M, El Omari K, Filman DJ, Schuermann JP, Hogle JM, Coen DM
EMBO J 34 2937-52 (2015)
PMID: 26511021

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147817 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nuclear egress protein 1 Chain: B
Molecule details ›
Chain: B
Length: 219 amino acids
Theoretical weight: 25.11 KDa
Source organism: Human herpesvirus 5 strain AD169
Expression system: Escherichia coli
UniProt:
  • Canonical: P16794 (Residues: 72-290; Coverage: 58%)
Gene names: NEC1, UL53
Sequence domains: Herpesvirus UL31-like protein

Ligands and Environments

1 bound ligand:
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P4
Unit cell:
a: 90.008Å b: 90.008Å c: 33.945Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.256 0.253 0.309
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Have NEC Coat, Will Travel: Structural Basis of Membrane Budding During Nuclear Egress in Herpesviruses.
Bigalke et al. (2017)
13 more