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1AJX

HIV-1 PROTEASE IN COMPLEX WITH THE CYCLIC UREA INHIBITOR AHA001

Summary for 1AJX
Entry DOI10.2210/pdb1ajx/pdb
DescriptorHIV-1 PROTEASE, AHA001 (3 entities in total)
Functional Keywordsprotease, aspartyl protease, non-peptide inhibitor, drug design, hiv-1
Biological sourceHuman immunodeficiency virus 1
Cellular locationMatrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential): P03366
Total number of polymer chains2
Total formula weight22146.15
Authors
Backbro, K.,Unge, T. (deposition date: 1997-05-11, release date: 1997-09-17, Last modification date: 2024-05-22)
Primary citationBackbro, K.,Lowgren, S.,Osterlund, K.,Atepo, J.,Unge, T.,Hulten, J.,Bonham, N.M.,Schaal, W.,Karlen, A.,Hallberg, A.
Unexpected binding mode of a cyclic sulfamide HIV-1 protease inhibitor.
J.Med.Chem., 40:898-902, 1997
Cited by
PubMed Abstract: Two cyclic, C2-symmetric HIV-1 protease inhibitors, one sulfamide and one urea derivative, both comprising phenyl ether groups in the P1/P1' positions, were cocrystallized with HIV-1 protease, and the crystal structures were determined to 2.0 A resolution. The structure of the urea 2 showed a conformation similar to that reported for the related urea 3 by Lam et al., while the sulfamide 1 adopted an unanticipated conformation in which the P1' and P2' side chains were transposed.
PubMed: 9083478
DOI: 10.1021/jm960588d
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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