|Entry||Database: PDB / ID: 1dif|
|Title||HIV-1 PROTEASE IN COMPLEX WITH A DIFLUOROKETONE CONTAINING INHIBITOR A79285|
|Function / homology|
Function and homology information
induction by virus of host cysteine-type endopeptidase activity involved in apoptotic process / HIV-1 retropepsin / retroviral ribonuclease H / exoribonuclease H / exoribonuclease H activity / host multivesicular body / DNA integration / RNA-directed DNA polymerase / viral penetration into host nucleus / viral genome integration into host DNA ...induction by virus of host cysteine-type endopeptidase activity involved in apoptotic process / HIV-1 retropepsin / retroviral ribonuclease H / exoribonuclease H / exoribonuclease H activity / host multivesicular body / DNA integration / RNA-directed DNA polymerase / viral penetration into host nucleus / viral genome integration into host DNA / RNA-directed DNA polymerase activity / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / establishment of integrated proviral latency / RNA-DNA hybrid ribonuclease activity / suppression by virus of host gene expression / viral entry into host cell / viral nucleocapsid / DNA recombination / lipid binding / Hydrolases; Acting on ester bonds / DNA-directed DNA polymerase / aspartic-type endopeptidase activity / DNA-directed DNA polymerase activity / host cell nucleus / host cell plasma membrane / virion membrane / structural molecule activity / RNA binding / DNA binding / zinc ion binding
Immunodeficiency lentiviral matrix, N-terminal / Ribonuclease H-like superfamily / Integrase, catalytic core / Integrase, C-terminal, retroviral / Retroviral nucleocapsid protein Gag / Reverse transcriptase domain / Peptidase A2A, retrovirus, catalytic / Ribonuclease H domain / Integrase, N-terminal zinc-binding domain / Retrovirus capsid, C-terminal ...Immunodeficiency lentiviral matrix, N-terminal / Ribonuclease H-like superfamily / Integrase, catalytic core / Integrase, C-terminal, retroviral / Retroviral nucleocapsid protein Gag / Reverse transcriptase domain / Peptidase A2A, retrovirus, catalytic / Ribonuclease H domain / Integrase, N-terminal zinc-binding domain / Retrovirus capsid, C-terminal / Retrovirus capsid, N-terminal / Reverse transcriptase connection / Reverse transcriptase thumb / Aspartic peptidase, active site / Retroviral matrix protein / Zinc finger, CCHC-type / Matrix protein, lentiviral and alpha-retroviral, N-terminal / Retropepsin-like catalytic domain / Retroviral aspartyl protease / Zinc finger, CCHC-type superfamily / Integrase-like, N-terminal / Ribonuclease H superfamily / Integrase, C-terminal domain superfamily, retroviral / Retropepsins / Aspartic peptidase domain superfamily / Cathepsin D, subunit A; domain 1 / Acid Proteases / Beta Barrel / Mainly Beta
|Biological species||Human immunodeficiency virus 1|
|Method||X-RAY DIFFRACTION / Resolution: 1.7 Å|
|Authors||Silva, A.M. / Cachau, R.E. / Sham, H.L. / Erickson, J.W.|
|Citation||Journal: J.Mol.Biol. / Year: 1996|
Title: Inhibition and catalytic mechanism of HIV-1 aspartic protease.
Authors: Silva, A.M. / Cachau, R.E. / Sham, H.L. / Erickson, J.W.
SummaryFull reportAbout validation report
|Structure viewer||Molecule: |
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A: HIV-1 PROTEASE
B: HIV-1 PROTEASE
Mass: 10803.756 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human immunodeficiency virus 1 / Genus: Lentivirus / Production host: Escherichia coli (E. coli) / References: UniProt: P03367
|#2: Chemical||#3: Chemical|| ChemComp-A85 / ||#4: Water|| ChemComp-HOH / |
|Experiment||Method: X-RAY DIFFRACTION|
|Crystal||Density Matthews: 2.24 Å3/Da / Density % sol: 45.01 %|
*PLUSpH: 6.2 / Method: vapor diffusion, hanging drop
|Components of the solutions|
|Diffraction source||Wavelength: 1.5418|
|Detector||Type: RIGAKU / Detector: IMAGE PLATE|
|Radiation||Monochromatic (M) / Laue (L): M / Scattering type: x-ray|
|Radiation wavelength||Wavelength: 1.5418 Å / Relative weight: 1|
|Reflection||Num. obs: 20479 / % possible obs: 94.9 % / Redundancy: 2 % / Rmerge(I) obs: 0.0094|
*PLUSHighest resolution: 1.7 Å / Num. measured all: 40709 / Rmerge(I) obs: 0.092
|Refinement||Resolution: 1.7→10 Å / σ(F): 3 / |
|Refinement step||Cycle: LAST / Resolution: 1.7→10 Å|
|Refine LS restraints|
*PLUSName: X-PLOR / Classification: refinement
|Refine LS restraints|
*PLUSType: x_dihedral_angle_deg / Dev ideal: 29.1
-Mar 5, 2020. Novel coronavirus structure data
Novel coronavirus structure data
- International Committee on Taxonomy of Viruses (ICTV) defined the short name of the 2019 coronavirus as "SARS-CoV-2".
The species Severe acute respiratory syndrome-related coronavirus: classifying 2019-nCoV and naming it SARS-CoV-2 - nature microbiology
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