eF-site ID 1k6t-AB
PDB Code 1k6t
Chain A, B

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Title LACK OF SYNERGY FOR INHIBITORS TARGETING A MULTI-DRUG RESISTANT HIV-1 PROTEASE
Classification HYDROLASE
Compound POL polyprotein
Source Human immunodeficiency virus type 1 group M subtype B (isolate YU-2) (HIV-1) (POL_HV1Y2)
Sequence A:  PQITLWKRPLVTIRIGGQLKEALLDTGADDTVLEEMNLPG
RWKPKMIGGIGGFIKVRQYDQIPIEICGHKAIGTVLVGPT
PTNVIGRNLLTQIGCTLNF
B:  PQITLWKRPLVTIRIGGQLKEALLDTGADDTVLEEMNLPG
RWKPKMIGGIGGFIKVRQYDQIPIEICGHKAIGTVLVGPT
PTNVIGRNLLTQIGCTLNF
Description


Functional site

1) chain A
residue 1
type
sequence P
description BINDING SITE FOR RESIDUE ACT A 502
source : AC1

2) chain B
residue 69
type
sequence H
description BINDING SITE FOR RESIDUE ACT A 502
source : AC1

3) chain B
residue 70
type
sequence K
description BINDING SITE FOR RESIDUE ACT A 502
source : AC1

4) chain A
residue 7
type
sequence K
description BINDING SITE FOR RESIDUE ACT A 503
source : AC2

5) chain A
residue 8
type
sequence R
description BINDING SITE FOR RESIDUE ACT A 503
source : AC2

6) chain B
residue 87
type
sequence R
description BINDING SITE FOR RESIDUE ACT A 503
source : AC2

7) chain A
residue 16
type
sequence G
description BINDING SITE FOR RESIDUE ACT A 506
source : AC3

8) chain A
residue 17
type
sequence G
description BINDING SITE FOR RESIDUE ACT A 506
source : AC3

9) chain B
residue 14
type
sequence R
description BINDING SITE FOR RESIDUE ACT A 506
source : AC3

10) chain B
residue 17
type
sequence G
description BINDING SITE FOR RESIDUE ACT A 506
source : AC3

11) chain B
residue 1
type
sequence P
description BINDING SITE FOR RESIDUE ACT B 508
source : AC4

12) chain B
residue 57
type
sequence R
description BINDING SITE FOR RESIDUE ACT B 508
source : AC4

13) chain B
residue 69
type
sequence H
description BINDING SITE FOR RESIDUE ACT B 508
source : AC4

14) chain A
residue 6
type
sequence W
description BINDING SITE FOR RESIDUE XN1 B 509
source : AC5

15) chain A
residue 8
type
sequence R
description BINDING SITE FOR RESIDUE XN1 B 509
source : AC5

16) chain A
residue 25
type
sequence D
description BINDING SITE FOR RESIDUE XN1 B 509
source : AC5

17) chain A
residue 48
type
sequence G
description BINDING SITE FOR RESIDUE XN1 B 509
source : AC5

18) chain A
residue 49
type
sequence G
description BINDING SITE FOR RESIDUE XN1 B 509
source : AC5

19) chain A
residue 50
type
sequence I
description BINDING SITE FOR RESIDUE XN1 B 509
source : AC5

20) chain A
residue 84
type
sequence V
description BINDING SITE FOR RESIDUE XN1 B 509
source : AC5

21) chain B
residue 25
type
sequence D
description BINDING SITE FOR RESIDUE XN1 B 509
source : AC5

22) chain B
residue 27
type
sequence G
description BINDING SITE FOR RESIDUE XN1 B 509
source : AC5

23) chain B
residue 28
type
sequence A
description BINDING SITE FOR RESIDUE XN1 B 509
source : AC5

24) chain B
residue 29
type
sequence D
description BINDING SITE FOR RESIDUE XN1 B 509
source : AC5

25) chain B
residue 30
type
sequence D
description BINDING SITE FOR RESIDUE XN1 B 509
source : AC5

26) chain B
residue 32
type
sequence V
description BINDING SITE FOR RESIDUE XN1 B 509
source : AC5

27) chain B
residue 48
type
sequence G
description BINDING SITE FOR RESIDUE XN1 B 509
source : AC5

28) chain B
residue 50
type
sequence I
description BINDING SITE FOR RESIDUE XN1 B 509
source : AC5

29) chain B
residue 81
type
sequence P
description BINDING SITE FOR RESIDUE XN1 B 509
source : AC5

30) chain A
residue 22-33
type prosite
sequence ALLDTGADDTVL
description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
source prosite : PS00141

31) chain A
residue 76
type SITE
sequence L
description Cleavage; by viral protease => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

32) chain B
residue 76
type SITE
sequence L
description Cleavage; by viral protease => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

33) chain A
residue 76
type MOD_RES
sequence L
description Phosphotyrosine; by host => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

34) chain B
residue 76
type MOD_RES
sequence L
description Phosphotyrosine; by host => ECO:0000250
source Swiss-Prot : SWS_FT_FI2


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