1wpo Summary

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HYDROLYTIC ENZYME HUMAN CYTOMEGALOVIRUS PROTEASE

The structure was published by Tong, L., Qian, C., Massariol, M.J., Bonneau, P.R., Cordingley, M.G., and Lagace, L., in 1996 in a paper entitled "A new serine-protease fold revealed by the crystal structure of human cytomegalovirus protease." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1996.

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

This PDB entry contains multiple copies of the structure of HUMAN CYTOMEGALOVIRUS PROTEASE.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

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 HUMAN CYTOMEGALOVIRUS PROTEASE P16753 (1-256) (SCAF_HCMVA)search Human herpesvirus 5 strain AD169search < 90% 256 82%
B HUMAN CYTOMEGALOVIRUS PROTEASE P16753 (1-256) (SCAF_HCMVA)search Human herpesvirus 5 strain AD169search < 90% 256 82%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P16753 (1 - 256) HUMAN CYTOMEGALOVIRUS PROTEASE Human herpesvirus 5

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B Herpes virus serine proteinase, assemblinsearch Serine Protease, Human Cytomegalovirus Protease; Chain Asearch 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