eF-site ID 1hmv-ABEF
PDB Code 1hmv
Chain A, B, E, F

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Title THE STRUCTURE OF UNLIGANDED REVERSE TRANSCRIPTASE FROM THE HUMAN IMMUNODEFICIENCY VIRUS TYPE 1
Classification NUCLEOTIDYLTRANSFERASE
Compound HIV-1 REVERSE TRANSCRIPTASE (SUBUNIT P66)
Source Human immunodeficiency virus type 1 group M subtype B (isolate BH10) (HIV-1) (POL_HV1B1)
Sequence A:  PISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTE
MEKEGKISKIGPENPYNTPVFAIVDFRELNKRTQDFWEVQ
LGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTAFT
IPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFKKQNPDI
VIYQYMDDLYVGSDLEIGQHRTKIEELRQHLLRWGLTTPD
KKHQKEPPFLWMGYELHPDKWTVQPIVLPEKDSWTVNDIQ
KLVGKLNWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEE
AELELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWT
YQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAVQKITTE
SIVIWGKTPKFKLPIQKETWETWWTEYWQATWIPEWEFVN
TPPLVKLWYQLEKEPIVGAETFYVDGAANRETKLGKAGYV
TNKGRQKVVPLTNTTNQKTELQAIYLALQDSGLEVNIVTD
SQYALGIIQAQPDKSESELVNQIIEQLIKKEKVYLAWVPA
HKGIGGNEQVDKLVSA
B:  IETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKE
GKISKIGPENPYNTPVFAIKKWRKLVDFRELNKRTQDFWE
VQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTA
FTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILE
PFKKQNPDIVIYQYMDDLYVGSDLEIGQHRTKIEELRQHL
LRHPDKWTVQPIVLPEKDSWTVNDIQKLVGKLNWASQIYP
GIKVRQLCKLLRGTKALTEVIPLTEEAELELAENREILKE
PVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTG
KYARMRGAHTNDVKQLTEAVQKITTESIVIWGKTPKFKLP
IQKETWETWWTEYWQATWIPEWEFVNTPPLVKLWY
E:  PISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTE
MEKEGKISKIGPENPYNTPVFAIVDFRELNKRTQDFWEVQ
LGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTAFT
IPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFKKQNPDI
VIYQYMDDLYVGSDLEIGQHRTKIEELRQHLLRWGLTTPD
KKHQKEPPFLWMGYELHPDKWTVQPIVLPEKDSWTVNDIQ
KLVGKLNWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEE
AELELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWT
YQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAVQKITTE
SIVIWGKTPKFKLPIQKETWETWWTEYWQATWIPEWEFVN
TPPLVKLWYQLEKEPIVGAETFYVDGAANRETKLGKAGYV
TNKGRQKVVPLTNTTNQKTELQAIYLALQDSGLEVNIVTD
SQYALGIIQAQPDKSESELVNQIIEQLIKKEKVYLAWVPA
HKGIGGNEQVDKLVSA
F:  IETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKE
GKISKIGPENPYNTPVFAIKKWRKLVDFRELNKRTQDFWE
VQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTA
FTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILE
PFKKQNPDIVIYQYMDDLYVGSDLEIGQHRTKIEELRQHL
LRHPDKWTVQPIVLPEKDSWTVNDIQKLVGKLNWASQIYP
GIKVRQLCKLLRGTKALTEVIPLTEEAELELAENREILKE
PVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTG
KYARMRGAHTNDVKQLTEAVQKITTESIVIWGKTPKFKLP
IQKETWETWWTEYWQATWIPEWEFVNTPPLVKLWY
Description


Functional site

1) chain A
residue 443
type
sequence D
description BINDING SITE FOR RESIDUE MG B 501
source : AC1

2) chain A
residue 478
type
sequence E
description BINDING SITE FOR RESIDUE MG B 501
source : AC1

3) chain A
residue 498
type
sequence D
description BINDING SITE FOR RESIDUE MG B 501
source : AC1

4) chain E
residue 443
type
sequence D
description BINDING SITE FOR RESIDUE MG F 501
source : AC3

5) chain E
residue 478
type
sequence E
description BINDING SITE FOR RESIDUE MG F 501
source : AC3

6) chain E
residue 498
type
sequence D
description BINDING SITE FOR RESIDUE MG F 501
source : AC3

7) chain A
residue 220
type MOD_RES
sequence K
description Asymmetric dimethylarginine; in Nucleocapsid protein p7; by host PRMT6 => ECO:0000269|PubMed:17415034
source Swiss-Prot : SWS_FT_FI10

8) chain A
residue 242
type MOD_RES
sequence Q
description Asymmetric dimethylarginine; in Nucleocapsid protein p7; by host PRMT6 => ECO:0000269|PubMed:17415034
source Swiss-Prot : SWS_FT_FI10

9) chain E
residue 220
type MOD_RES
sequence K
description Asymmetric dimethylarginine; in Nucleocapsid protein p7; by host PRMT6 => ECO:0000269|PubMed:17415034
source Swiss-Prot : SWS_FT_FI10

10) chain E
residue 242
type MOD_RES
sequence Q
description Asymmetric dimethylarginine; in Nucleocapsid protein p7; by host PRMT6 => ECO:0000269|PubMed:17415034
source Swiss-Prot : SWS_FT_FI10

11) chain B
residue 244-261
type ZN_FING
sequence IVLPEKDSWTVNDIQKLV
description CCHC-type 2 => ECO:0000255|PROSITE-ProRule:PRU00047
source Swiss-Prot : SWS_FT_FI2

12) chain F
residue 244-261
type ZN_FING
sequence IVLPEKDSWTVNDIQKLV
description CCHC-type 2 => ECO:0000255|PROSITE-ProRule:PRU00047
source Swiss-Prot : SWS_FT_FI2

13) chain B
residue 358
type ACT_SITE
sequence R
description For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000269|PubMed:12924029
source Swiss-Prot : SWS_FT_FI3

14) chain F
residue 358
type ACT_SITE
sequence R
description For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000269|PubMed:12924029
source Swiss-Prot : SWS_FT_FI3

15) chain B
residue 54
type SITE
sequence N
description Cis/trans isomerization of proline peptide bond; by human PPIA/CYPA => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

16) chain F
residue 54
type SITE
sequence N
description Cis/trans isomerization of proline peptide bond; by human PPIA/CYPA => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

17) chain B
residue 196
type SITE
sequence G
description Cleavage; by viral protease => ECO:0000250
source Swiss-Prot : SWS_FT_FI5

18) chain B
residue 210
type SITE
sequence L
description Cleavage; by viral protease => ECO:0000250
source Swiss-Prot : SWS_FT_FI5

19) chain F
residue 196
type SITE
sequence G
description Cleavage; by viral protease => ECO:0000250
source Swiss-Prot : SWS_FT_FI5

20) chain F
residue 210
type SITE
sequence L
description Cleavage; by viral protease => ECO:0000250
source Swiss-Prot : SWS_FT_FI5

21) chain B
residue 265
type SITE
sequence N
description Cleavage; by viral protease => ECO:0000255
source Swiss-Prot : SWS_FT_FI6

22) chain F
residue 265
type SITE
sequence N
description Cleavage; by viral protease => ECO:0000255
source Swiss-Prot : SWS_FT_FI6

23) chain E
residue 196
type SITE
sequence G
description Cleavage; by viral protease => ECO:0000255
source Swiss-Prot : SWS_FT_FI6

24) chain E
residue 210
type SITE
sequence L
description Cleavage; by viral protease => ECO:0000255
source Swiss-Prot : SWS_FT_FI6

25) chain B
residue 273
type SITE
sequence G
description Cleavage; by viral protease
source Swiss-Prot : SWS_FT_FI7

26) chain B
residue 333
type SITE
sequence G
description Cleavage; by viral protease
source Swiss-Prot : SWS_FT_FI7

27) chain F
residue 273
type SITE
sequence G
description Cleavage; by viral protease
source Swiss-Prot : SWS_FT_FI7

28) chain F
residue 333
type SITE
sequence G
description Cleavage; by viral protease
source Swiss-Prot : SWS_FT_FI7

29) chain E
residue 273
type SITE
sequence G
description Cleavage; by viral protease => ECO:0000269|PubMed:2476069
source Swiss-Prot : SWS_FT_FI8

30) chain E
residue 333
type SITE
sequence G
description Cleavage; by viral protease => ECO:0000269|PubMed:2476069
source Swiss-Prot : SWS_FT_FI8

31) chain B
residue 242
type MOD_RES
sequence Q
description Asymmetric dimethylarginine; in Nucleocapsid protein p7; by host PRMT6 => ECO:0000269|PubMed:17415034
source Swiss-Prot : SWS_FT_FI9

32) chain F
residue 242
type MOD_RES
sequence Q
description Asymmetric dimethylarginine; in Nucleocapsid protein p7; by host PRMT6 => ECO:0000269|PubMed:17415034
source Swiss-Prot : SWS_FT_FI9


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