eF-site ID 1rqi-A
PDB Code 1rqi
Chain A

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Title Active Conformation of Farnesyl Pyrophosphate Synthase Bound to Isopentyl Pyrophosphate and Dimethylallyl S-Thiolodiphosphate
Classification TRANSFERASE
Compound Geranyltranstransferase
Source (ISPA_ECOLI)
Sequence A:  AMDFPQQLEACVKQANQALSRFIAPLPFQNTPVVETMQYG
ALLGGKRLRPFLVYATGHMFGVSTNTLDAPAAAVECIHAY
SLIHDDLPAMDDDDLRRGLPTCHVKFGEANAILAGDALQT
LAFSILSDADMPEVSDRDRISMISELASASGIAGMCGGQA
LDLDAEGKHVPLDALERIHRHKTGALIRAAVRLGALSAGD
KGRRALPVLDKYAESIGLAFQVQDDILDVVGDTATLGKRQ
GADQQLGKSTYPALLGLEQARKKARDLIDDARQSLKQLAE
QSLDTSALEALADYIIQRNK
Description


Functional site

1) chain A
residue 244
type
sequence D
description BINDING SITE FOR RESIDUE MG A 603
source : AC4

2) chain A
residue 105
type
sequence D
description BINDING SITE FOR RESIDUE MG A 604
source : AC5

3) chain A
residue 111
type
sequence D
description BINDING SITE FOR RESIDUE MG A 604
source : AC5

4) chain A
residue 105
type
sequence D
description BINDING SITE FOR RESIDUE MG A 605
source : AC6

5) chain A
residue 111
type
sequence D
description BINDING SITE FOR RESIDUE MG A 605
source : AC6

6) chain A
residue 113
type
sequence D
description BINDING SITE FOR RESIDUE MG A 605
source : AC6

7) chain A
residue 101
type
sequence S
description BINDING SITE FOR RESIDUE DST A 401
source : AC8

8) chain A
residue 102
type
sequence L
description BINDING SITE FOR RESIDUE DST A 401
source : AC8

9) chain A
residue 105
type
sequence D
description BINDING SITE FOR RESIDUE DST A 401
source : AC8

10) chain A
residue 111
type
sequence D
description BINDING SITE FOR RESIDUE DST A 401
source : AC8

11) chain A
residue 116
type
sequence R
description BINDING SITE FOR RESIDUE DST A 401
source : AC8

12) chain A
residue 175
type
sequence M
description BINDING SITE FOR RESIDUE DST A 401
source : AC8

13) chain A
residue 179
type
sequence Q
description BINDING SITE FOR RESIDUE DST A 401
source : AC8

14) chain A
residue 202
type
sequence K
description BINDING SITE FOR RESIDUE DST A 401
source : AC8

15) chain A
residue 244
type
sequence D
description BINDING SITE FOR RESIDUE DST A 401
source : AC8

16) chain A
residue 258
type
sequence K
description BINDING SITE FOR RESIDUE DST A 401
source : AC8

17) chain A
residue 65
type
sequence G
description BINDING SITE FOR RESIDUE IPR A 501
source : BC1

18) chain A
residue 66
type
sequence K
description BINDING SITE FOR RESIDUE IPR A 501
source : BC1

19) chain A
residue 69
type
sequence R
description BINDING SITE FOR RESIDUE IPR A 501
source : BC1

20) chain A
residue 98
type
sequence H
description BINDING SITE FOR RESIDUE IPR A 501
source : BC1

21) chain A
residue 117
type
sequence R
description BINDING SITE FOR RESIDUE IPR A 501
source : BC1

22) chain A
residue 203
type
sequence T
description BINDING SITE FOR RESIDUE IPR A 501
source : BC1

23) chain A
residue 240
type
sequence F
description BINDING SITE FOR RESIDUE IPR A 501
source : BC1

24) chain A
residue 241
type
sequence Q
description BINDING SITE FOR RESIDUE IPR A 501
source : BC1

25) chain A
residue 244
type
sequence D
description BINDING SITE FOR RESIDUE IPR A 501
source : BC1

26) chain A
residue 27
type
sequence Q
description BINDING SITE FOR RESIDUE DPO A 606
source : BC2

27) chain A
residue 30
type
sequence A
description BINDING SITE FOR RESIDUE DPO A 606
source : BC2

28) chain A
residue 31
type
sequence C
description BINDING SITE FOR RESIDUE DPO A 606
source : BC2

29) chain A
residue 34
type
sequence Q
description BINDING SITE FOR RESIDUE DPO A 606
source : BC2

30) chain A
residue 71
type
sequence F
description BINDING SITE FOR RESIDUE DPO A 606
source : BC2

31) chain A
residue 74
type
sequence Y
description BINDING SITE FOR RESIDUE DPO A 606
source : BC2

32) chain A
residue 75
type
sequence A
description BINDING SITE FOR RESIDUE DPO A 606
source : BC2

33) chain A
residue 78
type
sequence H
description BINDING SITE FOR RESIDUE DPO A 606
source : BC2

34) chain A
residue 236-248
type prosite
sequence IGLAFQVQDDILD
description POLYPRENYL_SYNTHASE_2 Polyprenyl synthases signature 2. IGlaFQVqDDIlD
source prosite : PS00444

35) chain A
residue 102-118
type prosite
sequence LIHDDLPAMDDDDLRRG
description POLYPRENYL_SYNTHASE_1 Polyprenyl synthases signature 1. LIhDDlpamDdddlRRG
source prosite : PS00723

36) chain A
residue 66
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:14672944
source Swiss-Prot : SWS_FT_FI1

37) chain A
residue 69
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:14672944
source Swiss-Prot : SWS_FT_FI1

38) chain A
residue 98
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:14672944
source Swiss-Prot : SWS_FT_FI1

39) chain A
residue 105
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:14672944
source Swiss-Prot : SWS_FT_FI1

40) chain A
residue 111
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:14672944
source Swiss-Prot : SWS_FT_FI1

41) chain A
residue 117
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:14672944
source Swiss-Prot : SWS_FT_FI1

42) chain A
residue 116
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI2

43) chain A
residue 202
type BINDING
sequence K
description
source Swiss-Prot : SWS_FT_FI2

44) chain A
residue 203
type BINDING
sequence T
description
source Swiss-Prot : SWS_FT_FI2

45) chain A
residue 241
type BINDING
sequence Q
description
source Swiss-Prot : SWS_FT_FI2

46) chain A
residue 258
type BINDING
sequence K
description
source Swiss-Prot : SWS_FT_FI2


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