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- PDB-2hpf: COMPARISON OF THE STRUCTURES OF HIV-2 PROTEASE COMPLEXES IN THREE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2hpf | ||||||
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Title | COMPARISON OF THE STRUCTURES OF HIV-2 PROTEASE COMPLEXES IN THREE CRYSTAL SPACE GROUPS WITH AN HIV-1 PROTEASE COMPLEX STRUCTURE | ||||||
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![]() | HYDROLASE(ACID PROTEASE) | ||||||
Function / homology | ![]() HIV-2 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-2 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 | ![]() | ||||||
![]() | Mulichak, A.M. / Watenpaugh, K.D. | ||||||
![]() | ![]() Title: Comparison of the Structures of HIV-2 Protease Complexes in Three Crystal Space Groups with an HIV-1 Protease Complex Structure Authors: Mulichak, A.M. / Watenpaugh, K.D. #1: ![]() Title: The Crystallographic Structure of the Protease from Human Immunodeficiency Virus Type 2 with Two Synthetic Peptidic Transition State Analog Inhibitors Authors: Mulichak, A.M. / Hui, J.O. / Tomasselli, A.G. / Heinrikson, R.L. / Curry, K.A. / Tomich, C.-S. / Thaisrivongs, S. / Sawyer, T.K. / Watenpaugh, K.D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 49.8 KB | Display | ![]() |
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PDB format | ![]() | 35.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 378.3 KB | Display | ![]() |
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Full document | ![]() | 399.3 KB | Display | |
Data in XML | ![]() | 9.1 KB | Display | |
Data in CIF | ![]() | 13.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein | Mass: 10712.315 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein/peptide | | Mass: 698.854 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source #3: Water | ChemComp-HOH / | Sequence details | THERE IS A PEPTIDE FRAGMENT IN THE SUBSTRATE BINDING POCKET. BECAUSE THE SIDE GROUPS ARE NOT KNOWN ...THERE IS A PEPTIDE FRAGMENT IN THE SUBSTRATE BINDING POCKET. BECAUSE THE SIDE GROUPS ARE NOT KNOWN FOR CERTAIN, THE RESIDUES HAVE ALL BEEN REPRESENTE | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.98 Å3/Da / Density % sol: 58.75 % |
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 3→40 Å / Num. obs: 5337 / % possible obs: 99 % / Observed criterion σ(F): 0 |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||
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Refinement | Resolution: 3→10 Å / σ(F): 2 Details: ATOMS WITH B-FACTORS GREATER THAN 70.0 A**2 MAY BE CONSIDERED TO BE DISORDERED OR NOT SEEN IN THE ELECTRON DENSITY MAPS.
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Refinement step | Cycle: LAST / Resolution: 3→10 Å
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