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- PDB-1hef: The crystal structures at 2.2 angstroms resolution of hydroxyethy... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1hef | |||||||||
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Title | The crystal structures at 2.2 angstroms resolution of hydroxyethylene-based inhibitors bound to human immunodeficiency virus type 1 protease show that the inhibitors are present in two distinct orientations | |||||||||
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![]() | HYDROLASE/HYDROLASE INHIBITOR / HYDROLASE-HYDROLASE INHIBITOR COMPLEX | |||||||||
Function / homology | ![]() HIV-1 retropepsin / symbiont-mediated activation of host apoptosis / retroviral ribonuclease H / exoribonuclease H / exoribonuclease H activity / host multivesicular body / DNA integration / viral genome integration into host DNA / RNA-directed DNA polymerase / establishment of integrated proviral latency ...HIV-1 retropepsin / symbiont-mediated activation of host apoptosis / retroviral ribonuclease H / exoribonuclease H / exoribonuclease H activity / host multivesicular body / DNA integration / viral genome integration into host DNA / RNA-directed DNA polymerase / establishment of integrated proviral latency / viral penetration into host nucleus / RNA stem-loop binding / symbiont-mediated suppression of host gene expression / RNA-directed DNA polymerase activity / host cell / RNA-DNA hybrid ribonuclease activity / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / viral nucleocapsid / aspartic-type endopeptidase activity / DNA recombination / DNA-directed DNA polymerase / Hydrolases; Acting on ester bonds / DNA-directed DNA polymerase activity / symbiont entry into host cell / lipid binding / host cell nucleus / host cell plasma membrane / structural molecule activity / virion membrane / proteolysis / DNA binding / zinc ion binding / membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Murthy, K. / Winborne, E.L. / Minnich, M.D. / Culp, J.S. / Debouck, C. | |||||||||
![]() | ![]() Title: The crystal structures at 2.2-A resolution of hydroxyethylene-based inhibitors bound to human immunodeficiency virus type 1 protease show that the inhibitors are present in two distinct orientations. Authors: Murthy, K.H. / Winborne, E.L. / Minnich, M.D. / Culp, J.S. / Debouck, C. | |||||||||
History |
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Remark 300 | HIV-1 PROTEASE IS A SYMMETRIC DIMER, WHILE THE INHIBITOR IS AN ASYMMETRIC MOLECULE. FURTHERMORE, ...HIV-1 PROTEASE IS A SYMMETRIC DIMER, WHILE THE INHIBITOR IS AN ASYMMETRIC MOLECULE. FURTHERMORE, THE INHIBITOR IS SMALL ENOUGH TO BE ENTIRELY CONTAINED WITHIN THE ACTIVE SITE OF THE ENZYME AND, THEREFORE, DOES NOT CONTRIBUTE TO INTER-DIMER CONTACTS. THUS, OF THE TWO POSSIBLE ORIENTATIONS OF THE INHIBITOR, NEITHER IS THERMODYNAMICALLY PREFERRED. IN THE CRYSTAL STRUCTURE, THEREFORE, BOTH ARE REPRESENTED EQUALLY. THE ASYMMETRIC UNIT OF THE CRYSTAL THUS CONSISTS OF ONE PROTEASE MONOMER, AND ONE COPY OF EACH OF TWO POSSIBLE ORIENTATIONS OF THE INHIBITOR. EACH COPY OF THE INHIBITOR REPRESENTS HALF THE TOTAL OCCUPANCY FOR THE INHIBITOR. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 36 KB | Display | ![]() |
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PDB format | ![]() | 22.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 384.7 KB | Display | ![]() |
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Full document | ![]() | 395.3 KB | Display | |
Data in XML | ![]() | 6.3 KB | Display | |
Data in CIF | ![]() | 7.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 10786.663 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein/peptide | |
#3: Water | ChemComp-HOH / |
Sequence details | THIS VARIANT OF THE HIV 1 PROTEASE HAS ASN AT THE POSITION 36 IN CHAIN E AS CONFIRMED BY INSPECTION ...THIS VARIANT OF THE HIV 1 PROTEASE HAS ASN AT THE POSITION 36 IN CHAIN E AS CONFIRMED BY INSPECTION |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.09 Å3/Da / Density % sol: 41.08 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 2.2→5 Å / σ(I): 2 Details: THE INHIBITOR ALA-ALA-PJJ-VAL-VME IS DISORDERED AROUND THE TWO-FOLD CYRSTALLOGRAPHIC AXIS. APPLICATION OF CRYSTALLOGRAPHIC SYMMETRY RESULTS IN THE OVERLAP OF THE TWO ORIENTATIONS. THE ...Details: THE INHIBITOR ALA-ALA-PJJ-VAL-VME IS DISORDERED AROUND THE TWO-FOLD CYRSTALLOGRAPHIC AXIS. APPLICATION OF CRYSTALLOGRAPHIC SYMMETRY RESULTS IN THE OVERLAP OF THE TWO ORIENTATIONS. THE OCCUPANCY OF EACH ORIENTATION IS 1/2.
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Refinement step | Cycle: LAST / Resolution: 2.2→5 Å
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Refine LS restraints |
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Software | *PLUS Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.159 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |