1T7K

Crystal Structure of HIV Protease complexed with Arylsulfonamide azacyclic urea

PDB DOI: https://doi.org/10.2210/pdb1T7K/pdb

Classification: HYDROLASE
Organism(s): Human immunodeficiency virus 1
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2004-05-10 Released: 2004-10-05
Deposition Author(s): Huang, P.P., Randolph, J.T., Klein, L.L., Vasavanonda, S., Dekhtyar, T., Stoll, V.S., Kempf, D.J.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.10 Å
R-Value Free: 0.277
R-Value Work: 0.254
R-Value Observed: 0.400

wwPDB Validation 3D Report Full Report

This is version 1.3 of the entry. See complete history.

Literature

Synthesis and Antiviral Activity of P1' Arylsulfonamide Azacyclic Urea HIV Protease Inhibitors

Huang, P.P., Randolph, J.T., Klein, L.L., Vasavanonda, S., Dekhtyar, T., Stoll, V.S., Kempf, D.J.

(2004) Bioorg Med Chem Lett 14: 4075-4078

PubMed: 15225729 Search on PubMed
DOI: https://doi.org/10.1016/j.bmcl.2004.05.036
Primary Citation of Related Structures:
1T7K

PubMed Abstract:
A series of novel azacyclic urea HIV protease inhibitors bearing a benzenesulfonamide group at P1' were synthesized utilizing a parallel synthesis method. Structural studies of early analogs bound in the enzyme active site were used to design more potent inhibitors. The effects of substituting the P1' benzenesulfonyl group on antiviral activity and protein binding are described.

Organizational Affiliation

Abbott Laboratories, Infectious Disease Research, Dept. R47D, Building AP52N, 200 Abbott Park Road, Abbott Park, IL 60064-6217, USA. peggy.huang@abbott.com

Macromolecule Content

Total Structure Weight: 22.21 kDa
Atom Count: 1,671
Modelled Residue Count: 198
Deposited Residue Count: 198
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Pol polyprotein [Contains: Protease (Retropepsin)]	A, B	99	Human immunodeficiency virus 1	Mutation(s): 0 Gene Names: POL EC: 3.4.23.16
UniProt
Find proteins for P03366 (Human immunodeficiency virus type 1 group M subtype B (isolate BH10)) Explore P03366 Go to UniProtKB: P03366
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P03366
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
BH0 Query on BH0 Download Ideal Coordinates CCD File SDF format, chain C [auth B] MOL2 format, chain C [auth B]	C [auth B]	3-({5-BENZYL-6-HYDROXY-2,4-BIS-(4-HYDROXY-BENZYL)-3-OXO-[1,2,4]-TRIAZEPANE-1-SULFONYL)-BENZONITRILE C₃₂ H₃₀ N₄ O₆ S UYUWNNRWESUYOB-FIRIVFDPSA-N		Interactions Focus chain C [auth B]

Binding Affinity Annotations
ID	Source	Binding Affinity
BH0	Binding MOAD: 1T7K	Ki: 1.37 (nM) from 1 assay(s)

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.10 Å
R-Value Free: 0.277
R-Value Work: 0.254
R-Value Observed: 0.400
Space Group: P 2₁ 2₁ 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 57.326	α = 90
b = 86.001	β = 90
c = 46.077	γ = 90

Software Package:

Software Name	Purpose
HKL-2000	data collection
SCALEPACK	data scaling
CNS	refinement
HKL-2000	data reduction
CNS	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2004-10-05

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2004-10-05
Type: Initial release
Version 1.1: 2008-04-30
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2024-02-14
Changes: Data collection, Database references, Derived calculations