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- PDB-3jsm: K65R mutant HIV-1 reverse transcriptase cross-linked to DS-DNA an... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3jsm | ||||||
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Title | K65R mutant HIV-1 reverse transcriptase cross-linked to DS-DNA and complexed with tenofovir-diphosphate as the incoming nucleotide substrate | ||||||
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![]() | TRANSFERASE/DNA COMPLEX / HIV-1 REVERSE TRANSCRIPTASE / TENOFOVIR / RT-DNA COMPLEX / TRANSFERASE-DNA COMPLEX / DRUG RESISTANCE MUTATION / AIDS / DNA RECOMBINATION / DNA-DIRECTED DNA POLYMERASE / RNASE H / HYDROLASE / LIPOPROTEIN / MAGNESIUM / MEMBRANE / METAL-BINDING / MULTIFUNCTIONAL ENZYME / NUCLEOTIDYLTRANSFERASE / RNA-DIRECTED DNA POLYMERASE TRANSFERASE / TRANSFERASE-DNA COMPLEX complex | ||||||
Function / homology | ![]() 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 | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Das, K. / Arnold, E. | ||||||
![]() | ![]() Title: Structural basis for the role of the K65r mutation in HIV-1 reverse transcriptase polymerization, excision antagonism, and tenofovir resistance. Authors: Das, K. / Bandwar, R.P. / White, K.L. / Feng, J.Y. / Sarafianos, S.G. / Tuske, S. / Tu, X. / Clark, A.D. / Boyer, P.L. / Hou, X. / Gaffney, B.L. / Jones, R.A. / Miller, M.D. / Hughes, S.H. / Arnold, E. #1: ![]() Title: Structures of HIV-1 RT-DNA Complexes Before and After Incorporation of the Anti-Aids Drug Tenofovir Authors: Tuske, S. / Sarafianos, S.G. / Clark Jr., A.D. / Ding, J. / Naeger, L.K. / White, K.L. / Miller, M.D. / Gibbs, C.S. / Boyer, P.L. / Clark, P. / Wang, G. / Gaffney, B.L. / Jones, R.A. / ...Authors: Tuske, S. / Sarafianos, S.G. / Clark Jr., A.D. / Ding, J. / Naeger, L.K. / White, K.L. / Miller, M.D. / Gibbs, C.S. / Boyer, P.L. / Clark, P. / Wang, G. / Gaffney, B.L. / Jones, R.A. / Jerina, D.M. / Hughes, S.H. / Arnold, E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 238.4 KB | Display | ![]() |
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PDB format | ![]() | 185.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 779.7 KB | Display | ![]() |
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Full document | ![]() | 853.8 KB | Display | |
Data in XML | ![]() | 46.8 KB | Display | |
Data in CIF | ![]() | 63.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3jytC ![]() 1t05S 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
-DNA chain , 2 types, 2 molecules TP
#1: DNA chain | Mass: 8383.385 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: Chemically modified with Thiol-DGMP and enzymatically terminated with DDGTP |
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#2: DNA chain | Mass: 6474.268 Da / Num. of mol.: 1 / Source method: obtained synthetically |
-HIV-1 REVERSE TRANSCRIPTASE ... , 2 types, 2 molecules AB
#3: Protein | Mass: 64277.676 Da / Num. of mol.: 1 / Mutation: K65R, Q258C, C280S Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#4: Protein | Mass: 51095.617 Da / Num. of mol.: 1 / Mutation: C280S Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
-Non-polymers , 4 types, 6 molecules ![](data/chem/img/TNV.gif)
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#5: Chemical | ChemComp-TNV / [ | ||||
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#6: Chemical | #7: Chemical | #8: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 5 Å3/Da / Density % sol: 75.38 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.4 Details: 10% PEG 8000, 100 MM AMMONIUM SULFATE, 20 MM MGCL2, 5% GLYCEROL, 5% SUCROSE, pH 6.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 270 / Detector: CCD / Date: Jun 17, 2007 |
Radiation | Monochromator: Horizontal bent Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9179 Å / Relative weight: 1 |
Reflection | Resolution: 3→50 Å / Num. obs: 49501 / % possible obs: 95.8 % / Observed criterion σ(I): -1 / Biso Wilson estimate: 53 Å2 / Rmerge(I) obs: 0.156 / Net I/σ(I): 5.6 |
Reflection shell | Resolution: 3→3.11 Å / Rmerge(I) obs: 0.563 / % possible all: 82.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1T05 Resolution: 3→49.17 Å / Rfactor Rfree error: 0.007 / Data cutoff high absF: 4226829.05 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: ENGH & HUBER / Details: BULK SOLVENT MODEL USED
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 41.38 Å2 / ksol: 0.3 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 3→49.17 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3→3.19 Å / Rfactor Rfree error: 0.023 / Total num. of bins used: 6
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Xplor file |
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