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

The structure was published by Khayat, R., Batra, R., Massariol, M.J., Lagace, L., and Tong, L., in 2001 in a paper entitled "Investigating the role of histidine 157 in the catalytic activity of human cytomegalovirus protease." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 2001.

The experimental data on which the structure is based was not deposited.

This PDB entry contains multiple copies of the structure of CAPSID PROTEIN P40: ASSEMBLIN PROTEASE.

The molecule most likely forms homodimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A CAPSID PROTEIN P40: ASSEMBLIN PROTEASE P16753 (1-256) (SCAF_HCMVA)search Human herpesvirus 5 strain AD169search < 90% 256 85%
B CAPSID PROTEIN P40: ASSEMBLIN PROTEASE P16753 (1-256) (SCAF_HCMVA)search Human herpesvirus 5 strain AD169search < 90% 256 85%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P16753 (1 - 256) CAPSID PROTEIN P40: ASSEMBLIN PROTEASE Human herpesvirus 5 strain AD169

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B Herpes virus serine proteinase, assemblinsearch Herpes virus serine proteinase, assemblinsearch Assemblin (Peptidase family S21)search

Chain ID Molecular function (GO) Biological process (GO)
A, B (P16753) serine-type endopeptidase activitysearch proteolysissearch

Chain InterPro annotation
A, B Peptidase S21search