Structure analysis

CRYSTAL STRUCTURE OF THE CATALYTIC SITE MUTANT (H157A) OF THE HUMAN CYTOMEGALOVIRUS PROTEASE

X-ray diffraction
2.2Å resolution
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 18040.23 Å2
Buried surface area: 3037.82 Å2
Dissociation area: 1,518.91 Å2
Dissociation energy (ΔGdiss): 11.44 kcal/mol
Dissociation entropy (TΔSdiss): 12.76 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-147808

Macromolecules

Chains: A, B
Length: 256 amino acids
Theoretical weight: 28.22 KDa
Source organism: Human herpesvirus 5 strain AD169
Expression system: Escherichia coli
UniProt:
  • Canonical: P16753 (Residues: 1-256; Coverage: 36%)
Gene names: APNG, UL80
Pfam: Assemblin (Peptidase family S21)
InterPro:
CATH: Herpesvirus/Caudovirus protease domain
SCOP: Herpes virus serine proteinase, assemblin

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