+Open data
-Basic information
Entry | Database: PDB / ID: 1eet | ||||||
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Title | HIV-1 REVERSE TRANSCRIPTASE IN COMPLEX WITH THE INHIBITOR MSC204 | ||||||
Components | (HIV-1 REVERSE TRANSCRIPTASEReverse transcriptase) x 2 | ||||||
Keywords | Viral protein / transferase / Heterodimer / protein-inhibitor complex | ||||||
Function / homology | Function and homology information : / : / HIV-1 retropepsin / retroviral ribonuclease H / exoribonuclease H / exoribonuclease H activity / host multivesicular body / DNA integration / RNA-directed DNA polymerase / viral penetration into host nucleus ...: / : / HIV-1 retropepsin / retroviral ribonuclease H / exoribonuclease H / exoribonuclease H activity / host multivesicular body / DNA integration / RNA-directed DNA polymerase / viral penetration into host nucleus / viral genome integration into host DNA / establishment of integrated proviral latency / RNA-directed DNA polymerase activity / RNA-DNA hybrid ribonuclease activity / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / viral nucleocapsid / DNA recombination / Hydrolases; Acting on ester bonds / DNA-directed DNA polymerase / aspartic-type endopeptidase activity / DNA-directed DNA polymerase activity / symbiont entry into host cell / symbiont-mediated suppression of host gene expression / lipid binding / host cell nucleus / host cell plasma membrane / virion membrane / structural molecule activity / proteolysis / DNA binding / RNA binding / zinc ion binding / membrane Similarity search - Function | ||||||
Biological species | Human immunodeficiency virus 1 | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.73 Å | ||||||
Authors | Hogberg, M. / Sahlberg, C. / Engelhardt, P. / Noreen, R. / Kangasmetsa, J. / Johansson, N.G. / Oberg, B. / Vrang, L. / Zhang, H. / Sahlberg, B.L. ...Hogberg, M. / Sahlberg, C. / Engelhardt, P. / Noreen, R. / Kangasmetsa, J. / Johansson, N.G. / Oberg, B. / Vrang, L. / Zhang, H. / Sahlberg, B.L. / Unge, T. / Lovgren, S. / Fridborg, K. / Backbro, K. | ||||||
Citation | Journal: J.Med.Chem. / Year: 1999 Title: Urea-PETT compounds as a new class of HIV-1 reverse transcriptase inhibitors. 3. Synthesis and further structure-activity relationship studies of PETT analogues. Authors: Hogberg, M. / Sahlberg, C. / Engelhardt, P. / Noreen, R. / Kangasmetsa, J. / Johansson, N.G. / Oberg, B. / Vrang, L. / Zhang, H. / Sahlberg, B.L. / Unge, T. / Lovgren, S. / Fridborg, K. / Backbro, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1eet.cif.gz | 204.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1eet.ent.gz | 162 KB | Display | PDB format |
PDBx/mmJSON format | 1eet.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ee/1eet ftp://data.pdbj.org/pub/pdb/validation_reports/ee/1eet | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 64160.551 Da / Num. of mol.: 1 / Fragment: RESIDUES 1-557 / Mutation: E478Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human immunodeficiency virus 1 / Genus: Lentivirus / Gene: BH10 / Plasmid: PET11C / Production host: Escherichia coli (E. coli) / References: UniProt: P03366, RNA-directed DNA polymerase |
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#2: Protein | Mass: 49927.422 Da / Num. of mol.: 1 / Fragment: RESIDUES 1001-1427 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human immunodeficiency virus 1 / Genus: Lentivirus / Gene: BH10 / Plasmid: PET11C / Production host: Escherichia coli (E. coli) / References: UniProt: P03366, RNA-directed DNA polymerase |
#3: Chemical | ChemComp-BFU / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 3 |
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-Sample preparation
Crystal | Density Matthews: 3.2 Å3/Da / Density % sol: 61.59 % |
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Crystal grow | Temperature: 294 K / Method: vapor diffusion, hanging drop / pH: 7.2 Details: Ammonium Sulfate, Potassium chloride, HEPES, Magnesium Chloride , pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 294K |
Crystal grow | *PLUS Method: unknownDetails: This particular structure is not described in this paper. |
-Data collection
Diffraction | Mean temperature: 279 K |
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Diffraction source | Source: SYNCHROTRON / Site: LURE / Beamline: D41A / Wavelength: 1.375 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jul 9, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.375 Å / Relative weight: 1 |
Reflection | Resolution: 2.73→47.5 Å / Num. all: 39238 / Num. obs: 36910 / % possible obs: 94.1 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 1.9 % / Biso Wilson estimate: 53.9 Å2 / Rmerge(I) obs: 0.102 / Net I/σ(I): 7.2 |
Reflection shell | Resolution: 2.73→2.9 Å / Redundancy: 1.6 % / Rmerge(I) obs: 0.558 / Num. unique all: 5540 / % possible all: 88.4 |
-Processing
Software |
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Refinement | Resolution: 2.73→47.5 Å / Rfactor Rfree error: 0.006 / Data cutoff high absF: 2977863.03 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 40.6 Å2 / ksol: 0.315 e/Å3 | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 51.5 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.73→47.5 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.73→2.9 Å / Rfactor Rfree error: 0.024 / Total num. of bins used: 6
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Xplor file |
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Software | *PLUS Name: CNS / Version: 0.9 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS σ(F): 0 / % reflection Rfree: 5.1 % | ||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 51.5 Å2 | ||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.381 / % reflection Rfree: 4.6 % / Rfactor Rwork: 0.33 |