4Q1W

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	10833.8	2	UniProt (V5Y949) Pfam (PF00077) UniProt (by SIFTS) (P04585) In PDB	Human immunodeficiency virus 1	Pol protein
2	A, B	PHOSPHATE ION	non-polymer		95.0	4	Chemie (PO4)
3	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)
4	B	ACETATE ION	non-polymer		59.0	1	Chemie (ACT)
5		water	water		18.0	109	Chemie (HOH)

Sequence modifications

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

PDB	External Database	Details
Lys 7	Gln 7	engineered mutation
Met 90	Leu 90	engineered mutation

Contents of the asymmetric unit

Polymers	Number of chains	2
	Total formula weight	21667.7
Non-Polymers*	Number of molecules	6
	Total formula weight	986.6
All*	Total formula weight	22654.2

*Water molecules are not included.