4Q1Y

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

Entity

Entity ID	Chain ID	Description	Type	Chain length	Formula weight	Number of molecules	DB Name (Accession)	Biological source	Descriptive keywords
1	A, B	aspartyl protease	polymer	99	10863.8	2	UniProt (V5Y949) Pfam (PF00077) UniProt (by SIFTS) (P04585) In PDB	Human immunodeficiency virus 1	Pol protein
2	A	PHOSPHATE ION	non-polymer		95.0	3	Chemie (PO4)
3	A, B	ACETATE ION	non-polymer		59.0	3	Chemie (ACT)
4	A	(3R,3AS,6AR)-HEXAHYDROFURO[2,3-B]FURAN-3-YL(1S,2R)-3-[[(4-AMINOPHENYL)SULFONYL](ISOBUTYL)AMINO]-1-BENZYL-2-HYDROXYPROPYLCARBAMATE	non-polymer		547.7	1	Chemie (017)
5		water	water		18.0	124	Chemie (HOH)

Sequence modifications

A, B: 1 - 99 (UniProt: V5Y949)

PDB	External Database	Details
Lys 7	Gln 7	engineered mutation
Ile 32	Val 32	engineered mutation
Phe 33	Leu 33	engineered mutation

Contents of the asymmetric unit

Polymers	Number of chains	2
	Total formula weight	21727.7
Non-Polymers*	Number of molecules	7
	Total formula weight	1009.7
All*	Total formula weight	22737.4

*Water molecules are not included.