eF-site ID 4q1w-AB PDB Code 4q1w 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:  PQITLWKRPLVTIRIGGQLKEALLDTGADDTVLEEMNLPG KWKPKMIGGIGGFIKVRQYDQIPIEICGHKAIGTVLVGPT PVNIIGRNLMTQIGCTLNF B:  PQITLWKRPLVTIRIGGQLKEALLDTGADDTVLEEMNLPG KWKPKMIGGIGGFIKVRQYDQIPIEICGHKAIGTVLVGPT PVNIIGRNLMTQIGCTLNF 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 16 type sequence G description BINDING SITE FOR RESIDUE PO4 A 101 source : AC1 5) chain A residue 20 type sequence K description BINDING SITE FOR RESIDUE PO4 A 102 source : AC2 6) chain A residue 21 type sequence E description BINDING SITE FOR RESIDUE PO4 A 102 source : AC2 7) chain A residue 36 type sequence M description BINDING SITE FOR RESIDUE PO4 A 103 source : AC3 8) chain A residue 37 type sequence N description BINDING SITE FOR RESIDUE PO4 A 103 source : AC3 9) chain B residue 39 type sequence P description BINDING SITE FOR RESIDUE PO4 A 103 source : AC3 10) chain B residue 40 type sequence G description BINDING SITE FOR RESIDUE PO4 A 103 source : AC3 11) chain A residue 25 type sequence D description BINDING SITE FOR RESIDUE 017 A 104 source : AC4 12) chain A residue 27 type sequence G description BINDING SITE FOR RESIDUE 017 A 104 source : AC4 13) chain A residue 28 type sequence A description BINDING SITE FOR RESIDUE 017 A 104 source : AC4 14) chain A residue 29 type sequence D description BINDING SITE FOR RESIDUE 017 A 104 source : AC4 15) chain A residue 30 type sequence D description BINDING SITE FOR RESIDUE 017 A 104 source : AC4 16) chain A residue 48 type sequence G description BINDING SITE FOR RESIDUE 017 A 104 source : AC4 17) chain A residue 49 type sequence G description BINDING SITE FOR RESIDUE 017 A 104 source : AC4 18) chain A residue 50 type sequence I description BINDING SITE FOR RESIDUE 017 A 104 source : AC4 19) chain B residue 25 type sequence D description BINDING SITE FOR RESIDUE 017 A 104 source : AC4 20) chain B residue 27 type sequence G description BINDING SITE FOR RESIDUE 017 A 104 source : AC4 21) chain B residue 28 type sequence A description BINDING SITE FOR RESIDUE 017 A 104 source : AC4 22) chain B residue 30 type sequence D description BINDING SITE FOR RESIDUE 017 A 104 source : AC4 23) chain B residue 48 type sequence G description BINDING SITE FOR RESIDUE 017 A 104 source : AC4 24) chain B residue 49 type sequence G description BINDING SITE FOR RESIDUE 017 A 104 source : AC4 25) chain B residue 81 type sequence P description BINDING SITE FOR RESIDUE 017 A 104 source : AC4 26) chain B residue 82 type sequence V description BINDING SITE FOR RESIDUE 017 A 104 source : AC4 27) chain A residue 87 type sequence R description BINDING SITE FOR RESIDUE PO4 B 101 source : AC5 28) chain B residue 6 type sequence W description BINDING SITE FOR RESIDUE PO4 B 101 source : AC5 29) chain B residue 7 type sequence K description BINDING SITE FOR RESIDUE PO4 B 101 source : AC5 30) chain B residue 8 type sequence R description BINDING SITE FOR RESIDUE PO4 B 101 source : AC5 31) chain A residue 49 type sequence G description BINDING SITE FOR RESIDUE ACT B 102 source : AC6 32) chain B residue 91 type sequence T description BINDING SITE FOR RESIDUE ACT B 102 source : AC6 33) chain B residue 92 type sequence Q description BINDING SITE FOR RESIDUE ACT B 102 source : AC6 34) chain A residue 25 type catalytic sequence D description 175 source MCSA : MCSA1 35) chain A residue 26 type catalytic sequence T description 175 source MCSA : MCSA1 36) chain A residue 27 type catalytic sequence G description 175 source MCSA : MCSA1 37) chain B residue 25 type catalytic sequence D description 175 source MCSA : MCSA2 38) chain B residue 26 type catalytic sequence T description 175 source MCSA : MCSA2 39) chain B residue 27 type catalytic sequence G description 175 source MCSA : MCSA2 40) 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 41) 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 42) chain A residue 99 type SITE sequence F description Cleavage; by viral protease => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 43) chain B residue 99 type SITE sequence F description Cleavage; by viral protease => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 44) chain A residue 22-33 type prosite sequence ALLDTGADDTVL description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL source prosite : PS00141

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