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

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Title Active Conformation of Farnesyl Pyrophosphate Synthase Bound to Isopentyl Pyrophosphate and Risedronate
Classification TRANSFERASE
Compound Geranyltranstransferase
Source null (ISPA_ECOLI)
Sequence A:  MDFPQQLEACVKQANQALSRFIAPLPFQNTPVVETMQYGA
LLGGKRLRPFLVYATGHMFGVSTNTLDAPAAAVECIHAYS
LIHDDLPAMDDDDLRRGLPTCHVKFGEANAILAGDALQTL
AFSILSDADMPEVSDRDRISMISELASASGIAGMCGGQAL
DLDAEGKHVPLDALERIHRHKTGALIRAAVRLGALSAGDK
GRRALPVLDKYAESIGLAFQVQDDILDVVGDTATLGKRQG
ADQQLGKSTYPALLGLEQARKKARDLIDDARQSLKQLAEQ
SLDTSALEALADYIIQRNK
Description


Functional site

1) chain A
residue 105
type
sequence D
description BINDING SITE FOR RESIDUE MG A 907
source : AC4

2) chain A
residue 111
type
sequence D
description BINDING SITE FOR RESIDUE MG A 907
source : AC4

3) chain A
residue 244
type
sequence D
description BINDING SITE FOR RESIDUE MG A 908
source : AC5

4) chain A
residue 105
type
sequence D
description BINDING SITE FOR RESIDUE MG A 909
source : AC6

5) chain A
residue 111
type
sequence D
description BINDING SITE FOR RESIDUE MG A 909
source : AC6

6) chain A
residue 65
type
sequence G
description BINDING SITE FOR RESIDUE IPE A 900
source : AC7

7) chain A
residue 66
type
sequence K
description BINDING SITE FOR RESIDUE IPE A 900
source : AC7

8) chain A
residue 69
type
sequence R
description BINDING SITE FOR RESIDUE IPE A 900
source : AC7

9) chain A
residue 98
type
sequence H
description BINDING SITE FOR RESIDUE IPE A 900
source : AC7

10) chain A
residue 117
type
sequence R
description BINDING SITE FOR RESIDUE IPE A 900
source : AC7

11) chain A
residue 203
type
sequence T
description BINDING SITE FOR RESIDUE IPE A 900
source : AC7

12) chain A
residue 240
type
sequence F
description BINDING SITE FOR RESIDUE IPE A 900
source : AC7

13) chain A
residue 241
type
sequence Q
description BINDING SITE FOR RESIDUE IPE A 900
source : AC7

14) chain A
residue 105
type
sequence D
description BINDING SITE FOR RESIDUE RIS A 901
source : AC8

15) chain A
residue 111
type
sequence D
description BINDING SITE FOR RESIDUE RIS A 901
source : AC8

16) chain A
residue 116
type
sequence R
description BINDING SITE FOR RESIDUE RIS A 901
source : AC8

17) chain A
residue 179
type
sequence Q
description BINDING SITE FOR RESIDUE RIS A 901
source : AC8

18) chain A
residue 202
type
sequence K
description BINDING SITE FOR RESIDUE RIS A 901
source : AC8

19) chain A
residue 203
type
sequence T
description BINDING SITE FOR RESIDUE RIS A 901
source : AC8

20) chain A
residue 241
type
sequence Q
description BINDING SITE FOR RESIDUE RIS A 901
source : AC8

21) chain A
residue 244
type
sequence D
description BINDING SITE FOR RESIDUE RIS A 901
source : AC8

22) chain A
residue 258
type
sequence K
description BINDING SITE FOR RESIDUE RIS A 901
source : AC8

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

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

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

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

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

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

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

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

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

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

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

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


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