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- PDB-1hhp: THE THREE-DIMENSIONAL STRUCTURE OF THE ASPARTYL PROTEASE FROM THE... -
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Basic information
Entry | Database: PDB / ID: 1hhp | ||||||
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Title | THE THREE-DIMENSIONAL STRUCTURE OF THE ASPARTYL PROTEASE FROM THE HIV-1 ISOLATE BRU | ||||||
![]() | UNLIGANDED HIV-1 PROTEASE | ||||||
![]() | HYDROLASE(ACID PROTEINASE) | ||||||
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 / DNA recombination / DNA-directed DNA polymerase / Hydrolases; Acting on ester bonds / aspartic-type endopeptidase activity / 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 | ![]() | ||||||
![]() | Spinelli, S. / Alzari, P.M. | ||||||
![]() | ![]() Title: The three-dimensional structure of the aspartyl protease from the HIV-1 isolate BRU. Authors: Spinelli, S. / Liu, Q.Z. / Alzari, P.M. / Hirel, P.H. / Poljak, R.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 29.8 KB | Display | ![]() |
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PDB format | ![]() | 19.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar 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
#1: Protein | Mass: 10803.756 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Genus: Lentivirus / Species: Human immunodeficiency virus 1 / Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.11 Å3/Da / Density % sol: 60.48 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / pH: 7 / 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 |
Reflection | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 6 Å / Num. obs: 3549 / % possible obs: 93 % / Observed criterion σ(F): 2 / Num. measured all: 3901 / Rmerge(I) obs: 0.098 |
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Processing
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Refinement | Rfactor Rwork: 0.19 / Highest resolution: 2.7 Å | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.7 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||
Refinement | *PLUS Lowest resolution: 6 Å / Num. reflection obs: 3549 / σ(F): 2 / Rfactor obs: 0.19 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS Biso mean: 31 Å2 | ||||||||||||
Refine LS restraints | *PLUS
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