eF-site ID 4q1y-AB PDB Code 4q1y 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:  PQITLWKRPLVTIRIGGQLKEALLDTGADDTIFEEMNLPG KWKPKMIGGIGGFIKVRQYDQIPIEICGHKAIGTVLVGPT PVNIIGRNLLTQIGCTLNF B:  PQITLWKRPLVTIRIGGQLKEALLDTGADDTIFEEMNLPG KWKPKMIGGIGGFIKVRQYDQIPIEICGHKAIGTVLVGPT PVNIIGRNLLTQIGCTLNF Description Functional site 1) chain A residue 14 type sequence R description BINDING SITE FOR RESIDUE PO4 A 101 source : AC1 2) chain A residue 16 type sequence G description BINDING SITE FOR RESIDUE PO4 A 101 source : AC1 3) chain A residue 17 type sequence G description BINDING SITE FOR RESIDUE PO4 A 101 source : AC1 4) chain B residue 14 type sequence R description BINDING SITE FOR RESIDUE PO4 A 101 source : AC1 5) chain B residue 16 type sequence G description BINDING SITE FOR RESIDUE PO4 A 101 source : AC1 6) chain A residue 6 type sequence W description BINDING SITE FOR RESIDUE PO4 A 102 source : AC2 7) chain A residue 49 type sequence G description BINDING SITE FOR RESIDUE PO4 A 102 source : AC2 8) chain A residue 53 type sequence F description BINDING SITE FOR RESIDUE PO4 A 102 source : AC2 9) chain B residue 81 type sequence P description BINDING SITE FOR RESIDUE PO4 A 102 source : AC2 10) chain B residue 92 type sequence Q description BINDING SITE FOR RESIDUE PO4 A 102 source : AC2 11) chain A residue 7 type sequence K description BINDING SITE FOR RESIDUE PO4 A 103 source : AC3 12) chain A residue 8 type sequence R description BINDING SITE FOR RESIDUE PO4 A 103 source : AC3 13) chain A residue 14 type sequence R description BINDING SITE FOR RESIDUE ACT A 104 source : AC4 14) chain A residue 19 type sequence L description BINDING SITE FOR RESIDUE ACT A 104 source : AC4 15) chain A residue 44 type sequence P description BINDING SITE FOR RESIDUE ACT A 104 source : AC4 16) chain A residue 45 type sequence K description BINDING SITE FOR RESIDUE ACT A 104 source : AC4 17) chain A residue 70 type sequence K description BINDING SITE FOR RESIDUE ACT A 105 source : AC5 18) chain B residue 1 type sequence P description BINDING SITE FOR RESIDUE ACT A 105 source : AC5 19) chain A residue 25 type sequence D description BINDING SITE FOR RESIDUE 017 A 106 source : AC6 20) chain A residue 27 type sequence G description BINDING SITE FOR RESIDUE 017 A 106 source : AC6 21) chain A residue 28 type sequence A description BINDING SITE FOR RESIDUE 017 A 106 source : AC6 22) chain A residue 29 type sequence D description BINDING SITE FOR RESIDUE 017 A 106 source : AC6 23) chain A residue 30 type sequence D description BINDING SITE FOR RESIDUE 017 A 106 source : AC6 24) chain A residue 48 type sequence G description BINDING SITE FOR RESIDUE 017 A 106 source : AC6 25) chain A residue 50 type sequence I description BINDING SITE FOR RESIDUE 017 A 106 source : AC6 26) chain B residue 25 type sequence D description BINDING SITE FOR RESIDUE 017 A 106 source : AC6 27) chain B residue 27 type sequence G description BINDING SITE FOR RESIDUE 017 A 106 source : AC6 28) chain B residue 28 type sequence A description BINDING SITE FOR RESIDUE 017 A 106 source : AC6 29) chain B residue 30 type sequence D description BINDING SITE FOR RESIDUE 017 A 106 source : AC6 30) chain B residue 48 type sequence G description BINDING SITE FOR RESIDUE 017 A 106 source : AC6 31) chain B residue 49 type sequence G description BINDING SITE FOR RESIDUE 017 A 106 source : AC6 32) chain B residue 50 type sequence I description BINDING SITE FOR RESIDUE 017 A 106 source : AC6 33) chain B residue 81 type sequence P description BINDING SITE FOR RESIDUE 017 A 106 source : AC6 34) chain B residue 82 type sequence V description BINDING SITE FOR RESIDUE 017 A 106 source : AC6 35) chain B residue 73 type sequence G description BINDING SITE FOR RESIDUE ACT B 101 source : AC7 36) chain B residue 74 type sequence T description BINDING SITE FOR RESIDUE ACT B 101 source : AC7 37) chain B residue 88 type sequence N description BINDING SITE FOR RESIDUE ACT B 101 source : AC7 38) chain A residue 22-33 type prosite sequence ALLDTGADDTIF description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTIF source prosite : PS00141 39) chain A residue 25 type catalytic sequence D description 175 source MCSA : MCSA1 40) chain A residue 26 type catalytic sequence T description 175 source MCSA : MCSA1 41) chain A residue 27 type catalytic sequence G description 175 source MCSA : MCSA1 42) chain B residue 25 type catalytic sequence D description 175 source MCSA : MCSA2 43) chain B residue 26 type catalytic sequence T description 175 source MCSA : MCSA2 44) chain B residue 27 type catalytic sequence G description 175 source MCSA : MCSA2 45) 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 46) 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 47) chain A residue 99 type SITE sequence F description Cleavage; by viral protease => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 48) 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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