eF-site ID 2f8z-F
PDB Code 2f8z
Chain F

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Title Crystal structure of human FPPS in complex with zoledronate and isopentenyl diphosphate
Classification TRANSFERASE
Compound Farnesyl Diphosphate Synthase
Source Homo sapiens (Human) (FPPS_HUMAN)
Sequence F:  DVYAQEKQDFVQHFSQIVRVLTEDEMGHPEIGDAIARLKE
VLEYNAIGGKYNRGLTVVVAFRELVEPRKQDADSLQRAWT
VGWCVELLQAFFLVADDIMDSSLTRRGQICWYQKPGVGLD
AINDANLLEACIYRLLKLYCREQPYYLNLIELFLQSSYQT
EIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFYSFY
LPIAAAMYMAGIDGEKEHANAKKILLEMGEFFQIQDDYLD
LFGDPSVTGKIGTDIQDNKCSWLVVQCLQRATPEQYQILK
ENYGQKEAEKVARVKALYEELDLPAVFLQYEEDSYSHIMA
LIEQYAAPLPPAVFLGLARKIYKRRK
Description


Functional site

1) chain F
residue 103
type
sequence D
description BINDING SITE FOR RESIDUE MG F 1001
source : AC1

2) chain F
residue 107
type
sequence D
description BINDING SITE FOR RESIDUE MG F 1001
source : AC1

3) chain F
residue 243
type
sequence D
description BINDING SITE FOR RESIDUE MG F 1002
source : AC2

4) chain F
residue 103
type
sequence D
description BINDING SITE FOR RESIDUE MG F 1003
source : AC3

5) chain F
residue 107
type
sequence D
description BINDING SITE FOR RESIDUE MG F 1003
source : AC3

6) chain F
residue 56
type
sequence G
description BINDING SITE FOR RESIDUE IPE F 9001
source : AC4

7) chain F
residue 57
type
sequence K
description BINDING SITE FOR RESIDUE IPE F 9001
source : AC4

8) chain F
residue 60
type
sequence R
description BINDING SITE FOR RESIDUE IPE F 9001
source : AC4

9) chain F
residue 96
type
sequence Q
description BINDING SITE FOR RESIDUE IPE F 9001
source : AC4

10) chain F
residue 113
type
sequence R
description BINDING SITE FOR RESIDUE IPE F 9001
source : AC4

11) chain F
residue 201
type
sequence T
description BINDING SITE FOR RESIDUE IPE F 9001
source : AC4

12) chain F
residue 239
type
sequence F
description BINDING SITE FOR RESIDUE IPE F 9001
source : AC4

13) chain F
residue 240
type
sequence Q
description BINDING SITE FOR RESIDUE IPE F 9001
source : AC4

14) chain F
residue 243
type
sequence D
description BINDING SITE FOR RESIDUE IPE F 9001
source : AC4

15) chain F
residue 103
type
sequence D
description BINDING SITE FOR RESIDUE ZOL F 5001
source : AC5

16) chain F
residue 107
type
sequence D
description BINDING SITE FOR RESIDUE ZOL F 5001
source : AC5

17) chain F
residue 112
type
sequence R
description BINDING SITE FOR RESIDUE ZOL F 5001
source : AC5

18) chain F
residue 200
type
sequence K
description BINDING SITE FOR RESIDUE ZOL F 5001
source : AC5

19) chain F
residue 201
type
sequence T
description BINDING SITE FOR RESIDUE ZOL F 5001
source : AC5

20) chain F
residue 240
type
sequence Q
description BINDING SITE FOR RESIDUE ZOL F 5001
source : AC5

21) chain F
residue 243
type
sequence D
description BINDING SITE FOR RESIDUE ZOL F 5001
source : AC5

22) chain F
residue 257
type
sequence K
description BINDING SITE FOR RESIDUE ZOL F 5001
source : AC5

23) chain F
residue 123
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:16684881, ECO:0007744|PDB:1ZW5
source Swiss-Prot : SWS_FT_FI1

24) chain F
residue 126
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:16684881, ECO:0007744|PDB:1ZW5
source Swiss-Prot : SWS_FT_FI1

25) chain F
residue 162
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:16684881, ECO:0007744|PDB:1ZW5
source Swiss-Prot : SWS_FT_FI1

26) chain F
residue 169
type BINDING
sequence I
description BINDING => ECO:0000269|PubMed:16684881, ECO:0007744|PDB:1ZW5
source Swiss-Prot : SWS_FT_FI1

27) chain F
residue 173
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:16684881, ECO:0007744|PDB:1ZW5
source Swiss-Prot : SWS_FT_FI1

28) chain F
residue 179
type BINDING
sequence P
description BINDING => ECO:0000269|PubMed:16684881, ECO:0007744|PDB:1ZW5
source Swiss-Prot : SWS_FT_FI1

29) chain F
residue 178
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI2

30) chain F
residue 266
type BINDING
sequence K
description
source Swiss-Prot : SWS_FT_FI2

31) chain F
residue 267
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI2

32) chain F
residue 306
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI2

33) chain F
residue 323
type BINDING
sequence S
description
source Swiss-Prot : SWS_FT_FI2

34) chain F
residue 332
type BINDING
sequence Y
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

35) chain F
residue 164
type SITE
sequence S
description Important for determining product chain length => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

36) chain F
residue 165
type SITE
sequence Y
description Important for determining product chain length => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

37) chain F
residue 123
type MOD_RES
sequence G
description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI5

38) chain F
residue 353
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI6

39) chain F
residue 235-247
type prosite
sequence MGEFFQIQDDYLD
description POLYPRENYL_SYNTHASE_2 Polyprenyl synthases signature 2. MGefFQIqDDYlD
source prosite : PS00444

40) chain F
residue 100-114
type prosite
sequence LVADDIMDSSLTRRG
description POLYPRENYL_SYNTHASE_1 Polyprenyl synthases signature 1. LVaDDim..DssltRRG
source prosite : PS00723


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