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Yorodumi- PDB-4j54: Crystal Structure of Multidrug Resistant HIV-1 Protease Clinical ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4j54 | ||||||
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Title | Crystal Structure of Multidrug Resistant HIV-1 Protease Clinical isolate PR20 with the potent antiviral inhibitor GRL-0519A | ||||||
Components | Protease | ||||||
Keywords | HYDROLASE/HYDROLASE INHIBITOR / multidrug resistant HIV-1 protease clinical isolate PR20 / clinical inhibitor Amprenavir / potent antiviral inhibitor GRL-0519A / potent antiviral inhibitor GRL-02031 / HYDROLASE-HYDROLASE INHIBITOR complex | ||||||
Function / homology | Function and homology information HIV-1 retropepsin / 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 ...HIV-1 retropepsin / 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 / RNA-directed DNA polymerase activity / host cell / RNA-DNA hybrid ribonuclease activity / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / symbiont-mediated suppression of host gene expression / 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 | Human immunodeficiency virus 1 | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.55 Å | ||||||
Authors | Wang, Y.-F. / Agniswamy, J. / Weber, I.T. | ||||||
Citation | Journal: J.Med.Chem. / Year: 2013 Title: Extreme Multidrug Resistant HIV-1 Protease with 20 Mutations Is Resistant to Novel Protease Inhibitors with P1'-Pyrrolidinone or P2-Tris-tetrahydrofuran. Authors: Agniswamy, J. / Shen, C.H. / Wang, Y.F. / Ghosh, A.K. / Rao, K.V. / Xu, C.X. / Sayer, J.M. / Louis, J.M. / Weber, I.T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4j54.cif.gz | 58.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4j54.ent.gz | 40.5 KB | Display | PDB format |
PDBx/mmJSON format | 4j54.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4j54_validation.pdf.gz | 781.5 KB | Display | wwPDB validaton report |
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Full document | 4j54_full_validation.pdf.gz | 784.1 KB | Display | |
Data in XML | 4j54_validation.xml.gz | 11.9 KB | Display | |
Data in CIF | 4j54_validation.cif.gz | 15.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/j5/4j54 ftp://data.pdbj.org/pub/pdb/validation_reports/j5/4j54 | HTTPS FTP |
-Related structure data
Related structure data | 4j55C 4j5jC 2hs2S C: citing same article (ref.) 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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Unit cell |
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-Components
#1: Protein | Mass: 10766.542 Da / Num. of mol.: 2 / Fragment: UNP residues 501-599 Mutation: Q7K,L10F,I13V,I15V,D30N,V32I,L33F,E35D,M36I,S37N,I47V,I54L,Q58E,I62V,L63P,A71V,I84V,N88D,L89T,L90M Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human immunodeficiency virus 1 / Gene: pol / Plasmid: pET11a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P03367, HIV-1 retropepsin #2: Chemical | #3: Chemical | ChemComp-IOD / #4: Chemical | ChemComp-ACT / | #5: Water | ChemComp-HOH / | |
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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: 2.03 Å3/Da / Density % sol: 39.28 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 4.8 Details: 0.25 M potassium iodide, 0.1 M sodium acetate, pH 4.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 0.8 Å |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Aug 4, 2010 |
Radiation | Monochromator: Rosenbaum-Rock double-crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8 Å / Relative weight: 1 |
Reflection | Resolution: 1.55→50 Å / Num. all: 24299 / Num. obs: 24299 / % possible obs: 92.5 % / Redundancy: 6.1 % / Rmerge(I) obs: 0.069 / Net I/σ(I): 22.6 |
Reflection shell | Resolution: 1.55→1.61 Å / Redundancy: 1.8 % / Rmerge(I) obs: 0.265 / Mean I/σ(I) obs: 2.5 / % possible all: 50.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2HS2 Resolution: 1.55→10 Å / Num. parameters: 6784 / Num. restraintsaints: 6513 / Cross valid method: FREE R / σ(F): 0 / Stereochemistry target values: ENGH AND HUBER
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Solvent computation | Solvent model: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-228 | |||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 19.8692 Å2 | |||||||||||||||||||||||||||||||||
Refine analyze | Num. disordered residues: 3 / Occupancy sum hydrogen: 0 / Occupancy sum non hydrogen: 1653.65 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.55→10 Å
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Refine LS restraints |
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