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- PDB-1c6x: ALTERNATE BINDING SITE FOR THE P1-P3 GROUP OF A CLASS OF POTENT H... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1c6x | ||||||
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Title | ALTERNATE BINDING SITE FOR THE P1-P3 GROUP OF A CLASS OF POTENT HIV-1 PROTEASE INHIBITORS AS A RESULT OF CONCERTED STRUCTURAL CHANGE IN 80'S LOOP. | ||||||
![]() | PROTEIN (PROTEASE) | ||||||
![]() | HYDROLASE | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Munshi, S. | ||||||
![]() | ![]() Title: An alternate binding site for the P1-P3 group of a class of potent HIV-1 protease inhibitors as a result of concerted structural change in the 80s loop of the protease. Authors: Munshi, S. / Chen, Z. / Yan, Y. / Li, Y. / Olsen, D.B. / Schock, H.B. / Galvin, B.B. / Dorsey, B. / Kuo, L.C. #1: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 53.1 KB | Display | ![]() |
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PDB format | ![]() | 38.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 458.4 KB | Display | ![]() |
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Full document | ![]() | 462.3 KB | Display | |
Data in XML | ![]() | 6.7 KB | Display | |
Data in CIF | ![]() | 9.7 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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Unit cell |
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Components
#1: Protein | Mass: 10801.674 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: NY5 ISOLATE / Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: O09893, Hydrolases; Acting on peptide bonds (peptidases); Metalloendopeptidases #2: Chemical | ChemComp-3IN / | #3: Water | ChemComp-HOH / | Compound details | 9X MUTANT PROTEASE HAS NINE POINT MUTATIONS COMPARED TO WILD TYPE: ...9X MUTANT PROTEASE HAS NINE POINT MUTATIONS COMPARED TO WILD TYPE: L10V,K20M,L24I,S37D,M46I,I54V,L63P,A71V,V82T THERE IS ONE PROTEASE DIMER IN AN ASYMMETRIC | Nonpolymer details | L-739,622 IS N-[2(S)-CYCLOPENTYL-1(R)-HYDROXY-3(R)METHYL] -5-[(2(S)-TERTIARY-BUTYLAMINO-CARBONYL)-4- ...L-739,622 IS N-[2(S)-CYCLOPENTY | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.96 Å3/Da / Density % sol: 58.48 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Details: crystals obtained by co-crystallization at ph 5.2, using 0.6M NaCl as precipitating agent in 0.1M sodium acetate buffer. protein was at 5.5 mg/ml concentration | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 5 / Method: vapor diffusion, hanging dropDetails: inhibitor-protein mixture and the reservoir solution were mixed in a 1:1(v/v) ratio | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | Num. all: 79495 / Num. obs: 8318 / % possible obs: 88 % / Rmerge(I) obs: 0.051 |
Reflection shell | Resolution: 2.5→2.59 Å / % possible all: 84 |
Reflection | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 20 Å / Num. measured all: 79495 |
Reflection shell | *PLUS % possible obs: 84 % / Num. unique obs: 775 / Num. measured obs: 2887 / Rmerge(I) obs: 0.167 / Mean I/σ(I) obs: 4.5 |
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Processing
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Refinement | Resolution: 2.5→8 Å / Rfactor Rfree: 0.3 / Rfactor Rwork: 0.2 / Rfactor obs: 0.2 / σ(F): 2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→8 Å
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Refine LS restraints |
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