+Open data
-Basic information
Entry | Database: PDB / ID: 1gno | ||||||
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Title | HIV-1 PROTEASE (WILD TYPE) COMPLEXED WITH U89360E (INHIBITOR) | ||||||
Components | HIV-1 PROTEASE | ||||||
Keywords | HYDROLASE (ACID PROTEASE) / ASPARTIC PROTEASE / HIV / MUTANT / INHIBITOR / U-89360E | ||||||
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 genome integration into host DNA ...HIV-1 retropepsin / : / retroviral ribonuclease H / exoribonuclease H / : / exoribonuclease H activity / host multivesicular body / DNA integration / RNA-directed DNA polymerase / viral genome integration into host DNA / viral penetration into host nucleus / establishment of integrated proviral latency / RNA-directed DNA polymerase activity / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / RNA-DNA hybrid ribonuclease activity / 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 / structural molecule activity / host cell plasma membrane / virion membrane / proteolysis / DNA binding / RNA binding / zinc ion binding / membrane Similarity search - Function | ||||||
Biological species | Human immunodeficiency virus 1 | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.3 Å | ||||||
Authors | Hong, L. / Treharne, A. / Hartsuck, J.A. / Foundling, S. / Tang, J. | ||||||
Citation | Journal: Biochemistry / Year: 1996 Title: Crystal structures of complexes of a peptidic inhibitor with wild-type and two mutant HIV-1 proteases. Authors: Hong, L. / Treharne, A. / Hartsuck, J.A. / Foundling, S. / Tang, J. #1: Journal: Biochemistry / Year: 1995 Title: Effect of Point Mutations on the Kinetics and the Inhibition of Human Immunodeficiency Virus Type 1 Protease: Relationship to Drug Resistance Authors: Lin, Y. / Lin, X. / Hong, L. / Foundling, S. / Heinrikson, R.L. / Thaisrivongs, S. / Leelamanit, W. / Raterman, D. / Shah, M. / Dunn, B.M. / al., et | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1gno.cif.gz | 54.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1gno.ent.gz | 39.6 KB | Display | PDB format |
PDBx/mmJSON format | 1gno.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gn/1gno ftp://data.pdbj.org/pub/pdb/validation_reports/gn/1gno | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.49734, -0.86756, -0.00026), Vector: |
-Components
#1: Protein | Mass: 10803.756 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human immunodeficiency virus 1 / Genus: Lentivirus / Production host: Escherichia coli (E. coli) References: UniProt: P03368, UniProt: P03366*PLUS, RNA-directed DNA polymerase #2: Chemical | #3: Water | ChemComp-HOH / | Nonpolymer details | THERE ARE TWO ORIENTATIO | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.23 Å3/Da / Density % sol: 44.75 % | |||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.3 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ROTATING ANODE / Type: SIEMENS / Wavelength: 1.5418 |
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Detector | Type: SIEMENS / Detector: AREA DETECTOR |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→100 Å / % possible obs: 90.7 % / Rmerge(I) obs: 0.039 |
-Processing
Software |
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Refinement | Resolution: 2.3→8 Å / σ(F): 3 /
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Displacement parameters | Biso mean: 20.2 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→8 Å
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Refine LS restraints |
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Software | *PLUS Name: PROLSQ / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.174 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |