eF-site ID 4q1x-B PDB Code 4q1x Chain B click to enlarge Title Mutations Outside the Active Site of HIV-1 Protease Alter Enzyme Structure and Dynamic Ensemble of the Active Site to Confer Drug Resistance Classification hydrolase/hydrolase inhibitor Compound ASPARTYL PROTEASE Source (V5Y949_9HIV1) Sequence B:  PQITLWKRPLVTIRIGGQLKEALLDTGADDTILEEMNLPG KWKPKMIGGIGGFIKVRQYDQIPIEICGHKAIGTVLVGPT PVNIIGRNLLTQIGCTLNF Description Functional site 1) chain B residue 25 type sequence D description BINDING SITE FOR RESIDUE 017 A 101 source : AC1 2) chain B residue 27 type sequence G description BINDING SITE FOR RESIDUE 017 A 101 source : AC1 3) chain B residue 28 type sequence A description BINDING SITE FOR RESIDUE 017 A 101 source : AC1 4) chain B residue 30 type sequence D description BINDING SITE FOR RESIDUE 017 A 101 source : AC1 5) chain B residue 48 type sequence G description BINDING SITE FOR RESIDUE 017 A 101 source : AC1 6) chain B residue 49 type sequence G description BINDING SITE FOR RESIDUE 017 A 101 source : AC1 7) chain B residue 50 type sequence I description BINDING SITE FOR RESIDUE 017 A 101 source : AC1 8) chain B residue 82 type sequence V description BINDING SITE FOR RESIDUE 017 A 101 source : AC1 9) chain B residue 8 type sequence R description BINDING SITE FOR RESIDUE GOL A 102 source : AC2 10) chain B residue 16 type sequence G description BINDING SITE FOR RESIDUE PO4 B 101 source : AC3 11) chain B residue 25 type catalytic sequence D description 175 source MCSA : MCSA2 12) chain B residue 26 type catalytic sequence T description 175 source MCSA : MCSA2 13) chain B residue 27 type catalytic sequence G description 175 source MCSA : MCSA2 14) chain B residue 25 type ACT_SITE sequence D description For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000305|PubMed:33542150 source Swiss-Prot : SWS_FT_FI1 15) chain B residue 99 type SITE sequence F description Cleavage; by viral protease => ECO:0000250 source Swiss-Prot : SWS_FT_FI2

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