+
Open data
-
Basic information
Entry | Database: PDB / ID: 1hqe | ||||||
---|---|---|---|---|---|---|---|
Title | HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 | ||||||
![]() | (POL POLYPROTEIN) x 2 | ||||||
![]() | TRANSFERASE / NUCLEOTIDYLTRANSFERASE | ||||||
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 | ![]() ![]() ![]() | ||||||
![]() | Ding, J. / Hsiou, Y. / Arnold, E. | ||||||
![]() | ![]() Title: The Lys103Asn mutation of HIV-1 RT: a novel mechanism of drug resistance. Authors: Hsiou, Y. / Ding, J. / Das, K. / Clark Jr., A.D. / Boyer, P.L. / Lewi, P. / Janssen, P.A. / Kleim, J.P. / Rosner, M. / Hughes, S.H. / Arnold, E. #1: ![]() Title: Structure of Unliganded HIV-1 Reverse Transcriptase at 2.7 A Resolution: Implications of Conformational Changes for Polymerization and Inhibition Mechanisms Authors: Hsiou, Y. / Ding, J. / Das, K. / Clark Jr., A.D. / Hughes, S.H. / Arnold, E. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 204.7 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 163 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 417.5 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 440.8 KB | Display | |
Data in XML | ![]() | 22.4 KB | Display | |
Data in CIF | ![]() | 34.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1hpzC ![]() 1hquC ![]() 1dloS C: citing same article ( S: Starting model for refinement |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 64485.887 Da / Num. of mol.: 1 / Fragment: P66 SUBUNIT / Mutation: K103N, C280S Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
---|---|
#2: Protein | Mass: 50266.684 Da / Num. of mol.: 1 / Fragment: P51 SUBUNIT / Mutation: K103N, C280S Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 3.25 Å3/Da / Density % sol: 62.1 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.8 Details: Bis-Tris.propane, ammoniun sulfate, glycerol, PEG 8000, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 277K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 8 / Details: used microseeding | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 108 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jan 28, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.91 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→50 Å / Num. obs: 37652 / % possible obs: 92.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 8.6 % / Rmerge(I) obs: 0.101 / Net I/σ(I): 6.6 |
Reflection | *PLUS Lowest resolution: 50 Å |
Reflection shell | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 2.8 Å / % possible obs: 87.6 % / Rmerge(I) obs: 0.376 |
-
Processing
Software |
| |||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: PDB entry 1DLO Resolution: 2.7→25 Å / Isotropic thermal model: isotropic / σ(F): 2 / Stereochemistry target values: Engh and Huber
| |||||||||||||||||||||
Displacement parameters | Biso mean: 64.8 Å2 | |||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.7→25 Å
| |||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||
Software | *PLUS Name: ![]() | |||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 25 Å / σ(F): 2 / % reflection Rfree: 3.5 % / Rfactor obs: 0.25 / Rfactor Rwork: 0.25 | |||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 64.8 Å2 | |||||||||||||||||||||
Refine LS restraints | *PLUS
| |||||||||||||||||||||
LS refinement shell | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 2.8 Å / Rfactor Rfree: 0.385 / Rfactor obs: 0.359 |