1ied

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF THE CATALYTIC SITE MUTANT (H157E) OF THE HUMAN CYTOMEGALOVIRUS PROTEASE

Released:

Function and Biology Details

Reaction catalysed:
Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in the scaffold protein.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Assemblin Chains: A, B
Molecule details ›
Chains: A, B
Length: 256 amino acids
Theoretical weight: 28.12 KDa
Source organism: Human herpesvirus 5 strain AD169
Expression system: Escherichia coli
UniProt:
  • Canonical: P16753 (Residues: 1-256; Coverage: 36%)
Gene names: APNG, UL80
Sequence domains: Assemblin (Peptidase family S21)
Structure domains: Herpesvirus/Caudovirus protease domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 32-ID
Spacegroup: P41212
Unit cell:
a: 76.2Å b: 76.2Å c: 170.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.226 0.269
Expression system: Escherichia coli