eF-site ID 4q1x-AB
PDB Code 4q1x
Chain A, B

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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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