+Open data
-Basic information
Entry | Database: PDB / ID: 2wpo | ||||||
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Title | HCMV protease inhibitor complex | ||||||
Components | HUMAN CYTOMEGALOVIRUS PROTEASE | ||||||
Keywords | HYDROLASE/HYDROLASE INHIBITOR / VIRAL PROTEASE / HYDROLASE-HYDROLASE INHIBITOR complex / COAT PROTEIN / SERINE PROTEASE | ||||||
Function / homology | Function and homology information assemblin / viral release from host cell / host cell cytoplasm / serine-type endopeptidase activity / host cell nucleus / proteolysis / identical protein binding Similarity search - Function | ||||||
Biological species | Human herpesvirus 5 | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.7 Å | ||||||
Authors | Tong, L. / Qian, C. / Massariol, M.-J. / Deziel, R. / Yoakim, C. / Lagace, L. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 1998 Title: Conserved mode of peptidomimetic inhibition and substrate recognition of human cytomegalovirus protease. Authors: Tong, L. / Qian, C. / Massariol, M.J. / Deziel, R. / Yoakim, C. / Lagace, L. #1: Journal: Nature / Year: 1996 Title: A New Serine-Protease Fold Revealed by the Crystal Structure of Human Cytomegalovirus Protease Authors: Tong, L. / Qian, C. / Massariol, M.J. / Bonneau, P.R. / Cordingley, M.G. / Lagace, L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2wpo.cif.gz | 219.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2wpo.ent.gz | 182.4 KB | Display | PDB format |
PDBx/mmJSON format | 2wpo.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wp/2wpo ftp://data.pdbj.org/pub/pdb/validation_reports/wp/2wpo | HTTPS FTP |
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-Related structure data
Related structure data | 1wpoS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Details | THERE ARE FOUR MOLECULES IN THE ASYMMETRIC UNIT, FORMING TWO NON-CRYSTALLOGRAPHIC DIMERS. |
-Components
#1: Protein | Mass: 28178.676 Da / Num. of mol.: 4 / Mutation: A143Q, T181M, L229M Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human herpesvirus 5 / Production host: Escherichia coli (E. coli) References: UniProt: P16753, Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases #2: Chemical | ChemComp-01E / ( |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.71 Å3/Da / Density % sol: 54.62 % | |||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 / Details: pH 7.5 | |||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Wavelength: 1.5418 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→20 Å / Num. obs: 33502 / % possible obs: 93 % / Observed criterion σ(I): 1 / Redundancy: 4 % / Rmerge(I) obs: 0.078 |
Reflection | *PLUS Num. measured all: 275527 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1WPO Resolution: 2.7→6 Å / Cross valid method: THROUGHOUT / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 2.7→6 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: RESTRAINTS |