4RVJ

Crystal structure of multidrug-resistant clinical isolate A02 HIV-1 protease in complex with amprenavir

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.200 
  • R-Value Work: 0.171 
  • R-Value Observed: 0.172 

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Ligand Structure Quality Assessment 


This is version 1.1 of the entry. See complete history. 


Literature

Enhanced antiviral activity by the P2-tris-tetrahydrofuran moiety of GRL-0519, a novel nonpeptidic HIV-1 protease inhibitor (PI), against multi-PI-resistant and highly darunavir-resistant strains of HIV-1

Yedidi, R.S., Maeda, K., Aoki, M., Garimella, H., Rao, K.V., Akasapu, S., Davis, D.A., Kaufman, J.D., Das, D., Wingfield, P.T., Amano, M., Ghosh, A.K., Mitsuya, H.

To be published.

Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
HIV-1 protease
A, B, C, D
99Human immunodeficiency virus 1Mutation(s): 1 
Gene Names: pol
UniProt
Find proteins for Q9J006 (Human immunodeficiency virus 1)
Explore Q9J006 
Go to UniProtKB:  Q9J006
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9J006
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
478
Query on 478
Download Ideal Coordinates CCD File 
E [auth B],
F [auth D]		{3-[(4-AMINO-BENZENESULFONYL)-ISOBUTYL-AMINO]-1-BENZYL-2-HYDROXY-PROPYL}-CARBAMIC ACID TETRAHYDRO-FURAN-3-YL ESTER
C25 H35 N3 O6 S
YMARZQAQMVYCKC-OEMFJLHTSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
478 BindingDB:  4RVJ Ki: min: 7.00e-3, max: 57 (nM) from 9 assay(s)
Kd: min: 0.4, max: 0.59 (nM) from 2 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.200 
  • R-Value Work: 0.171 
  • R-Value Observed: 0.172 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 45.25α = 90
b = 57.31β = 90.01
c = 86.9γ = 90
Software Package:
Software NamePurpose
HKL-2000data collection
MOLREPphasing
PHENIXrefinement
MOSFLMdata reduction
SCALAdata scaling

Structure Validation

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Ligand Structure Quality Assessment 


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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2016-05-04
    Type: Initial release
  • Version 1.1: 2024-02-28
    Changes: Data collection, Database references, Derived calculations