eF-site ID 4q1x-AB PDB Code 4q1x Chain A, 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 A:  PQITLWKRPLVTIRIGGQLKEALLDTGADDTILEEMNLPG KWKPKMIGGIGGFIKVRQYDQIPIEICGHKAIGTVLVGPT PVNIIGRNLLTQIGCTLNF B:  PQITLWKRPLVTIRIGGQLKEALLDTGADDTILEEMNLPG KWKPKMIGGIGGFIKVRQYDQIPIEICGHKAIGTVLVGPT PVNIIGRNLLTQIGCTLNF Description Functional site 1) chain A residue 25 type sequence D description BINDING SITE FOR RESIDUE 017 A 101 source : AC1 2) chain A residue 27 type sequence G description BINDING SITE FOR RESIDUE 017 A 101 source : AC1 3) chain A residue 28 type sequence A description BINDING SITE FOR RESIDUE 017 A 101 source : AC1 4) chain A residue 29 type sequence D description BINDING SITE FOR RESIDUE 017 A 101 source : AC1 5) chain A residue 30 type sequence D description BINDING SITE FOR RESIDUE 017 A 101 source : AC1 6) chain A residue 48 type sequence G description BINDING SITE FOR RESIDUE 017 A 101 source : AC1 7) chain A residue 50 type sequence I description BINDING SITE FOR RESIDUE 017 A 101 source : AC1 8) chain B residue 25 type sequence D description BINDING SITE FOR RESIDUE 017 A 101 source : AC1 9) chain B residue 27 type sequence G description BINDING SITE FOR RESIDUE 017 A 101 source : AC1 10) chain B residue 28 type sequence A description BINDING SITE FOR RESIDUE 017 A 101 source : AC1 11) chain B residue 30 type sequence D description BINDING SITE FOR RESIDUE 017 A 101 source : AC1 12) chain B residue 48 type sequence G description BINDING SITE FOR RESIDUE 017 A 101 source : AC1 13) chain B residue 49 type sequence G description BINDING SITE FOR RESIDUE 017 A 101 source : AC1 14) chain B residue 50 type sequence I description BINDING SITE FOR RESIDUE 017 A 101 source : AC1 15) chain B residue 82 type sequence V description BINDING SITE FOR RESIDUE 017 A 101 source : AC1 16) chain A residue 29 type sequence D description BINDING SITE FOR RESIDUE GOL A 102 source : AC2 17) chain A residue 87 type sequence R description BINDING SITE FOR RESIDUE GOL A 102 source : AC2 18) chain B residue 8 type sequence R description BINDING SITE FOR RESIDUE GOL A 102 source : AC2 19) chain A residue 14 type sequence R description BINDING SITE FOR RESIDUE PO4 B 101 source : AC3 20) chain A residue 16 type sequence G description BINDING SITE FOR RESIDUE PO4 B 101 source : AC3 21) chain A residue 17 type sequence G description BINDING SITE FOR RESIDUE PO4 B 101 source : AC3 22) chain B residue 16 type sequence G description BINDING SITE FOR RESIDUE PO4 B 101 source : AC3 23) chain A residue 25 type catalytic sequence D description 175 source MCSA : MCSA1 24) chain A residue 26 type catalytic sequence T description 175 source MCSA : MCSA1 25) chain A residue 27 type catalytic sequence G description 175 source MCSA : MCSA1 26) chain B residue 25 type catalytic sequence D description 175 source MCSA : MCSA2 27) chain B residue 26 type catalytic sequence T description 175 source MCSA : MCSA2 28) chain B residue 27 type catalytic sequence G description 175 source MCSA : MCSA2 29) chain A residue 22-33 type prosite sequence ALLDTGADDTIL description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTIL source prosite : PS00141 30) chain A 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 31) 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 32) chain A residue 99 type SITE sequence F description Cleavage; by viral protease => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 33) 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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