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

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Title CRYSTAL STRUCTURE OF M184V MUTANT HIV-1 REVERSE TRANSCRIPTASE IN COMPLEX WITH NEVIRAPINE
Classification TRANSFERASE
Compound HIV-1 REVERSE TRANSCRIPTASE
Source Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1) (POL_HV1H2)
Sequence A:  PIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEK
EGKISKIGPENPYNTPVFAKLVDFRELNKRTQDFWEVQLG
IPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTAFTIP
SINNPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFRKQN
PDIVIYQYVDDLYVGSDLEIGQHRTKIEELRQHLLRWGLT
TPDKKHQKEPPFLWMGYELHPDKWTVQPIVLPEKDSWTVN
DIQKLVGKLNWASQIYPGIKVRQLXKLLRGTKALTEVIPL
TEEAELELAENREILKEPVHGVYYDPSKDLIAEIQKQGQG
QWTYQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAVQKI
TTESIVIWGKTPKFKLPIQKETWETWWTEYWQATWIPEWE
FVNTPPLVKLWYQLEKEPIVGAETFYVDAGYVTNRGRQKV
VTTNQKTELQAIYLALQDSGLEVNIVTDSQYALGIIQAQP
DQSESELVNQIIEQLIKKEKVYLAWVP
B:  ETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKEG
KISKIGPENPYNTPVFAIKKKDSTKWRKLVDFRELNKRTQ
DFWIPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTAF
TIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEP
FRKQNPDIVIYQYVDDLYVGSDLEIGQHRTKIEELRQHLL
RWGPPFLWMGYELHPDKWTVQPIVLPEKDSWTVNDIQKLV
GKLNWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEEAEL
ELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWTYQI
YQEPFKNLKTGKYARTNDVKQLTEAVQKITTESIVIWGKT
PKFKLPIQKETWETWWTEYWQATWIPEWEFVNTPPLVKLW
YQ
Description


Functional site

1) chain A
residue 461
type
sequence R
description BINDING SITE FOR RESIDUE PO4 A 1300
source : AC1

2) chain B
residue 13
type
sequence K
description BINDING SITE FOR RESIDUE PO4 A 1300
source : AC1

3) chain A
residue 436
type
sequence G
description BINDING SITE FOR RESIDUE PO4 A 1301
source : AC2

4) chain A
residue 437
type
sequence A
description BINDING SITE FOR RESIDUE PO4 A 1301
source : AC2

5) chain A
residue 438
type
sequence E
description BINDING SITE FOR RESIDUE PO4 A 1301
source : AC2

6) chain A
residue 460
type
sequence N
description BINDING SITE FOR RESIDUE PO4 A 1301
source : AC2

7) chain A
residue 461
type
sequence R
description BINDING SITE FOR RESIDUE PO4 A 1301
source : AC2

8) chain B
residue 288
type
sequence A
description BINDING SITE FOR RESIDUE PO4 A 1301
source : AC2

9) chain A
residue 100
type
sequence L
description BINDING SITE FOR RESIDUE NVP A 999
source : AC3

10) chain A
residue 101
type
sequence K
description BINDING SITE FOR RESIDUE NVP A 999
source : AC3

11) chain A
residue 103
type
sequence K
description BINDING SITE FOR RESIDUE NVP A 999
source : AC3

12) chain A
residue 106
type
sequence V
description BINDING SITE FOR RESIDUE NVP A 999
source : AC3

13) chain A
residue 179
type
sequence V
description BINDING SITE FOR RESIDUE NVP A 999
source : AC3

14) chain A
residue 181
type
sequence Y
description BINDING SITE FOR RESIDUE NVP A 999
source : AC3

15) chain A
residue 188
type
sequence Y
description BINDING SITE FOR RESIDUE NVP A 999
source : AC3

16) chain A
residue 190
type
sequence G
description BINDING SITE FOR RESIDUE NVP A 999
source : AC3

17) chain A
residue 235
type
sequence H
description BINDING SITE FOR RESIDUE NVP A 999
source : AC3

18) chain A
residue 236
type
sequence P
description BINDING SITE FOR RESIDUE NVP A 999
source : AC3

19) chain A
residue 318
type
sequence Y
description BINDING SITE FOR RESIDUE NVP A 999
source : AC3

20) chain B
residue 235-252
type ZN_FING
sequence HPDKWTVQPIVLPEKDSW
description CCHC-type 1 => ECO:0000255|PROSITE-ProRule:PRU00047
source Swiss-Prot : SWS_FT_FI1

21) chain B
residue 256-273
type ZN_FING
sequence DIQKLVGKLNWASQIYPG
description CCHC-type 2 => ECO:0000255|PROSITE-ProRule:PRU00047
source Swiss-Prot : SWS_FT_FI2

22) chain B
residue 66
type SITE
sequence K
description Cis/trans isomerization of proline peptide bond; by human PPIA/CYPA
source Swiss-Prot : SWS_FT_FI4

23) chain B
residue 208
type SITE
sequence H
description Cleavage; by viral protease => ECO:0000250
source Swiss-Prot : SWS_FT_FI5

24) chain B
residue 285
type SITE
sequence G
description Cleavage; by viral protease => ECO:0000250
source Swiss-Prot : SWS_FT_FI5

25) chain B
residue 238
type SITE
sequence K
description Cleavage; by viral protease => ECO:0000255
source Swiss-Prot : SWS_FT_FI6

26) chain B
residue 271
type SITE
sequence Y
description Cleavage; by viral protease => ECO:0000255
source Swiss-Prot : SWS_FT_FI6

27) chain B
residue 277
type SITE
sequence R
description Cleavage; by viral protease => ECO:0000255
source Swiss-Prot : SWS_FT_FI6

28) chain A
residue 432
type SITE
sequence E
description Cleavage; by viral protease => ECO:0000255
source Swiss-Prot : SWS_FT_FI6

29) chain B
residue 333
type SITE
sequence G
description Cleavage; by viral protease => ECO:0000305|PubMed:15183348
source Swiss-Prot : SWS_FT_FI7

30) chain A
residue 271
type SITE
sequence Y
description Cleavage; by viral protease => ECO:0000305|PubMed:15183348
source Swiss-Prot : SWS_FT_FI7

31) chain A
residue 277
type SITE
sequence R
description Cleavage; by viral protease => ECO:0000305|PubMed:15183348
source Swiss-Prot : SWS_FT_FI7

32) chain A
residue 333
type SITE
sequence G
description Cleavage; by viral protease => ECO:0000305|PubMed:15183348
source Swiss-Prot : SWS_FT_FI8


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