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- PDB-3s54: HIV-1 protease triple mutants V32I, I47V, V82I with antiviral dru... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3s54 | ||||||
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Title | HIV-1 protease triple mutants V32I, I47V, V82I with antiviral drug darunavir in space group P21212 | ||||||
![]() | Protease | ||||||
![]() | HYDROLASE/HYDROLASE INHIBITOR / DARUNAVIR / HIV/AIDS / drug resistance / aspartic protease / molecular recognition / HYDROLASE-HYDROLASE INHIBITOR complex | ||||||
Function / homology | ![]() aspartic-type endopeptidase activity / proteolysis / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Tie, Y.-F. / Wang, Y.-F. / Weber, I.T. | ||||||
![]() | ![]() Title: Critical differences in HIV-1 and HIV-2 protease specificity for clinical inhibitors. Authors: Tie, Y. / Wang, Y.F. / Boross, P.I. / Chiu, T.Y. / Ghosh, A.K. / Tozser, J. / Louis, J.M. / Harrison, R.W. / Weber, I.T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 108.2 KB | Display | ![]() |
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PDB format | ![]() | 82.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 3s43C ![]() 3s45C ![]() 3s53C ![]() 3s56C ![]() 2ienS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 10754.703 Da / Num. of mol.: 2 / Fragment: residues 500-598 / Mutation: Q7K, V32I, L33I, I47V, L63I, C67A, V82I, C95A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Non-polymers , 6 types, 167 molecules ![](data/chem/img/NA.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/017.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/ACT.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/017.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/ACT.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-NA / | ||||||||
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#3: Chemical | #4: Chemical | ChemComp-017 / ( | #5: Chemical | ChemComp-GOL / | #6: Chemical | ChemComp-ACT / | #7: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.71 Å3/Da / Density % sol: 54.63 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 4.6 Details: 2M NaCl,0.1M Sodium Acetate pH4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 90 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Mar 21, 2007 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.42→50 Å / Num. all: 45155 / Num. obs: 45155 / % possible obs: 90.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5.7 % / Rmerge(I) obs: 0.084 / Net I/σ(I): 16.2 |
Reflection shell | Resolution: 1.42→1.47 Å / Redundancy: 2.2 % / Rmerge(I) obs: 0.336 / Mean I/σ(I) obs: 3 / % possible all: 49.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2IEN Resolution: 1.42→10 Å / Num. parameters: 17160 / Num. restraintsaints: 24159 / Cross valid method: FREE R / σ(F): 0 / Stereochemistry target values: ENGH AND HUBER / Details: conjugage gradient minimization
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Refine analyze | Num. disordered residues: 27 / Occupancy sum hydrogen: 1606 / Occupancy sum non hydrogen: 1686.3 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.42→10 Å
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Refine LS restraints |
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