Brand  (β version)

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
Non-standard Residues
Code Name Show
CAS S-(dimethylarsenic)cysteine
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 1JQ6   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : HUMAN CYTOMEGALOVIRUS PROTEASE DIMER-INTERFACE MUTANT, S225Y
Release Data : 2001-09-12
Compound :
mol_id molecule chains synonym
1 ASSEMBLIN A PROTEASE
ec: 3.4.21.97
mutation: A143Q, S225Y
Source :
mol_id organism_scientific organism_common expression_system
1 Human herpesvirus 5  (taxid:10359) Human cytomegalovirus Escherichia coli  (taxid:562)
Authors : Batra, R., Khayat, R., Tong, L.
Keywords : Herpesvirus, cytomegalovirus, serine protease, dimerization, enzyme activity regulation, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 2.30 Å )
Citation :

Molecular mechanism for dimerization to regulate the catalytic activity of human cytomegalovirus protease.

Batra, R.,Khayat, R.,Tong, L.
(2001)  Nat.Struct.Biol.  8 : 810 - 817

PubMed: 11524687
DOI: 10.1038/nsb0901-810

Chain : A
UniProt : P16753 (SCAF_HCMVA)
Reaction: EC: Evidence:
Physiological Direction:
Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in the scaffold protein. 3.4.21.97 HAMAP-Rule:MF_04008
-