Brand  (β version)

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

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
0FP N-(6-aminohexanoyl)-3-methyl-L-valyl-3-methyl-L-valyl-N~1~-[(2s,3s)-3-hydroxy-4-oxo-4-{[(1r)-1-phenylpropyl]amino}butan-2-yl]-N~4~,N~4~-dimethyl-L-aspartamide
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 1JQ7   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : HCMV protease dimer-interface mutant, S225Y complexed to Inhibitor BILC 408
Release Data : 2001-09-12
Compound :
mol_id molecule chains synonym
1 ASSEMBLIN A,B 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-HYDROLASE INHIBITOR COMPLEX
Exp. method : X-RAY DIFFRACTION ( 3.00 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, B
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
-