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Yorodumi- PDB-1hsi: CRYSTAL STRUCTURE AT 1.9 ANGSTROMS RESOLUTION OF HUMAN IMMUNODEFI... -
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-Basic information
Entry | Database: PDB / ID: 1hsi | ||||||
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Title | CRYSTAL STRUCTURE AT 1.9 ANGSTROMS RESOLUTION OF HUMAN IMMUNODEFICIENCY VIRUS (HIV) II PROTEASE COMPLEXED WITH L-735,524, AN ORALLY BIOAVAILABLE INHIBITOR OF THE HIV PROTEASES | ||||||
Components | HIV-2 PROTEASE | ||||||
Keywords | HYDROLASE (ACID PROTEINASE) | ||||||
Function / homology | Function and homology information 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 / viral penetration into host nucleus / establishment of integrated proviral latency ...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 / viral penetration into host nucleus / establishment of integrated proviral latency / 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 / virion membrane / structural molecule activity / proteolysis / DNA binding / zinc ion binding / membrane Similarity search - Function | ||||||
Biological species | Human immunodeficiency virus 2 | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.5 Å | ||||||
Authors | Chen, Z. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 1994 Title: Crystal structure at 1.9-A resolution of human immunodeficiency virus (HIV) II protease complexed with L-735,524, an orally bioavailable inhibitor of the HIV proteases. Authors: Chen, Z. / Li, Y. / Chen, E. / Hall, D.L. / Darke, P.L. / Culberson, C. / Shafer, J.A. / Kuo, L.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1hsi.cif.gz | 49.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hsi.ent.gz | 36.3 KB | Display | PDB format |
PDBx/mmJSON format | 1hsi.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1hsi_validation.pdf.gz | 369 KB | Display | wwPDB validaton report |
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Full document | 1hsi_full_validation.pdf.gz | 375.7 KB | Display | |
Data in XML | 1hsi_validation.xml.gz | 5.9 KB | Display | |
Data in CIF | 1hsi_validation.cif.gz | 8.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hs/1hsi ftp://data.pdbj.org/pub/pdb/validation_reports/hs/1hsi | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 10728.337 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: ROD ISOLATE / Source: (gene. exp.) Human immunodeficiency virus 2 / Genus: Lentivirus / Gene: HIV-2 PROTEASE FROM THE ROD ISOLATE / Production host: Escherichia coli (E. coli) References: UniProt: P04584, Hydrolases; Acting on peptide bonds (peptidases); Aspartic endopeptidases #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.76 Å3/Da / Density % sol: 55.38 % | ||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / pH: 7.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.5 Å / Num. obs: 7188 / % possible obs: 94.5 % / Num. measured all: 26671 / Rmerge(I) obs: 0.0468 |
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-Processing
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Refinement | Rfactor Rwork: 0.166 / Rfactor obs: 0.166 / Highest resolution: 2.5 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.5 Å
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Refine LS restraints |
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