4Q1W

Mutations Outside the Active Site of HIV-1 Protease Alter Enzyme Structure and Dynamic Ensemble of the Active Site to Confer Drug Resistance

Summary for 4Q1W

Entry DOI	10.2210/pdb4q1w/pdb
Related	4Q1X 4Q1Y
Descriptor	ASPARTYL PROTEASE, PHOSPHATE ION, (3R,3AS,6AR)-HEXAHYDROFURO[2,3-B]FURAN-3-YL(1S,2R)-3-[[(4-AMINOPHENYL)SULFONYL](ISOBUTYL)AMINO]-1-BENZYL-2-HYDROXYPROPYLCARBAMATE, ... (5 entities in total)
Functional Keywords	hiv-1 protease, aids, inhibitor complex, aspartyl protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological source	Human immunodeficiency virus 1
Total number of polymer chains	2
Total formula weight	22654.25
Authors	Ragland, D.A.,Nalam, M.N.L.,Cao, H.,Nalivaika, E.A.,Cai, Y.,Kurt-Yilmaz, N.,Schiffer, C.A. (deposition date: 2014-04-04, release date: 2015-02-18, Last modification date: 2024-02-28)
Primary citation	Ragland, D.A.,Nalivaika, E.A.,Nalam, M.N.,Prachanronarong, K.L.,Cao, H.,Bandaranayake, R.M.,Cai, Y.,Kurt-Yilmaz, N.,Schiffer, C.A. Drug resistance conferred by mutations outside the active site through alterations in the dynamic and structural ensemble of HIV-1 protease. J.Am.Chem.Soc., 136:11956-11963, 2014 Cited by PubMed: 25091085 DOI: 10.1021/ja504096m PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.85 Å)

Structure validation