eF-site ID 2y0f-ABCD
PDB Code 2y0f
Chain A, B, C, D

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Title STRUCTURE OF GCPE (IspG) FROM THERMUS THERMOPHILUS HB27
Classification OXIDOREDUCTASE
Compound 4-HYDROXY-3-METHYLBUT-2-EN-1-YL DIPHOSPHATE SYNTHASE
Source (ISPG_THET2)
Sequence A:  MRRPTPTVYVGRVPIGGAHPIAVQSMTNTPTRDVEATTAQ
VLELHRAGSEIVRLTVNDEEAAKAVPEIKRRLLAEGVEVP
LVGDFHFNGHLLLRKYPKMAEALDKFRINPGTLGRGRHKD
EHFAEMIRIAMDLGKPVRIGANWGSLDPALLTELMDRNAS
RPEPKSAHEVVLEALVESAVRAYEAALEMGLGEDKLVLSA
KVSKARDLVWVYRELARRTQAPLHLGLTEAGMGVKGIVAS
AAALAPLLLEGIGDTIRVSLTPSPKEPRTKEVEVAQEILQ
ALGLRAFAPEVTSCPGCGRTTSTFFQELAEEVSRRLKERL
PEWRARYPGVEELKVAVMGCVVNGPGESKHAHIGISLPGA
GEEPKAPVYADGKLLTILKGEGIAEEFLRLVEDYVKTRFA
PKA
B:  MRRPTPTVYVGRVPIGGAHPIAVQSMTNTPTRDVEATTAQ
VLELHRAGSEIVRLTVNDEEAAKAVPEIKRRLLAEGVEVP
LVGDFHFNGHLLLRKYPKMAEALDKFRINPGEHFAEMIRI
AMDLGKPVRIGANWGSLDPALLTELMDRNASRPEPKSAHE
VVLEALVESAVRAYEAALEMGLGEDKLVLSAKVSKARDLV
WVYRELARRTQAPLHLGLTEAGMGVKGIVASAAALAPLLL
EGIGDTIRVSLTPSPKEPRTKEVEVAQEILQALGLRAFAP
EVTSCPGCGRTTSTFFQELAEEVSRRLKERLPEWRARYPG
VEELKVAVMGCVVNGPGESKHAHIGISLPGAGEEPKAPVY
ADGKLLTILKGEGIAEEFLRLVEDYVKTRFAPKA
C:  MRRPTPTVYVGRVPIGGAHPIAVQSMTNTPTRDVEATTAQ
VLELHRAGSEIVRLTVNDEEAAKAVPEIKRRLLAEGVEVP
LVGDFHFNGHLLLRKYPKMAEALDKFRINPGTLHFAEMIR
IAMDLGKPVRIGANWGSLDPALLTELMDRNASRPEPKSAH
EVVLEALVESAVRAYEAALEMGLGEDKLVLSAKVSKARDL
VWVYRELARRTQAPLHLGLTEAGMGVKGIVASAAALAPLL
LEGIGDTIRVSLTPEPRTKEVEVAQEILQALGLRAFAPEV
TSCPGCGRTTSTFFQELAEEVSRRLKERLPEWRARYPGVE
ELKVAVMGCVVNGPGESKHAHIGISLPGAGEEPKAPVYAD
GKLLTILKGEGIAEEFLRLVEDYVKTRFAPKA
D:  MRRPTPTVYVGRVPIGGAHPIAVQSMTNTPTRDVEATTAQ
VLELHRAGSEIVRLTVNDEEAAKAVPEIKRRLLAEGVEVP
LVGDFHFNGHLLLRKYPKMAEALDKFRINPEHFAEMIRIA
MDLGKPVRIGANWGSLDPALLTELMDRNASRPEPKSAHEV
VLEALVESAVRAYEAALEMGLGEDKLVLSAKVSKARDLVW
VYRELARRTQAPLHLGLTEAGMGVKGIVASAAALAPLLLE
GIGDTIRVSLTPSPKEPRTKEVEVAQEILQALGLRAFAPE
VTSCPGCGRTTSTFFQELAEEVSRRLKERLPEWRARYPGV
EELKVAVMGCVVNGPGESKHAHIGISLPGAGEEPKAPVYA
DGKLLTILKGEGIAEEFLRLVEDYVKTRFAPKA
Description


Functional site

1) chain A
residue 297
type
sequence C
description BINDING SITE FOR RESIDUE SF4 A 501
source : AC1

2) chain A
residue 298
type
sequence P
description BINDING SITE FOR RESIDUE SF4 A 501
source : AC1

3) chain A
residue 299
type
sequence G
description BINDING SITE FOR RESIDUE SF4 A 501
source : AC1

4) chain A
residue 300
type
sequence C
description BINDING SITE FOR RESIDUE SF4 A 501
source : AC1

5) chain A
residue 342
type
sequence G
description BINDING SITE FOR RESIDUE SF4 A 501
source : AC1

6) chain A
residue 343
type
sequence C
description BINDING SITE FOR RESIDUE SF4 A 501
source : AC1

7) chain A
residue 346
type
sequence N
description BINDING SITE FOR RESIDUE SF4 A 501
source : AC1

8) chain A
residue 350
type
sequence E
description BINDING SITE FOR RESIDUE SF4 A 501
source : AC1

9) chain B
residue 158
type
sequence M
description BINDING SITE FOR RESIDUE SF4 A 501
source : AC1

10) chain A
residue 158
type
sequence M
description BINDING SITE FOR RESIDUE SF4 B 501
source : AC2

11) chain B
residue 297
type
sequence C
description BINDING SITE FOR RESIDUE SF4 B 501
source : AC2

12) chain B
residue 300
type
sequence C
description BINDING SITE FOR RESIDUE SF4 B 501
source : AC2

13) chain B
residue 343
type
sequence C
description BINDING SITE FOR RESIDUE SF4 B 501
source : AC2

14) chain B
residue 346
type
sequence N
description BINDING SITE FOR RESIDUE SF4 B 501
source : AC2

15) chain B
residue 350
type
sequence E
description BINDING SITE FOR RESIDUE SF4 B 501
source : AC2

16) chain C
residue 297
type
sequence C
description BINDING SITE FOR RESIDUE SF4 C 501
source : AC3

17) chain C
residue 298
type
sequence P
description BINDING SITE FOR RESIDUE SF4 C 501
source : AC3

18) chain C
residue 300
type
sequence C
description BINDING SITE FOR RESIDUE SF4 C 501
source : AC3

19) chain C
residue 342
type
sequence G
description BINDING SITE FOR RESIDUE SF4 C 501
source : AC3

20) chain C
residue 343
type
sequence C
description BINDING SITE FOR RESIDUE SF4 C 501
source : AC3

21) chain C
residue 346
type
sequence N
description BINDING SITE FOR RESIDUE SF4 C 501
source : AC3

22) chain C
residue 350
type
sequence E
description BINDING SITE FOR RESIDUE SF4 C 501
source : AC3

23) chain D
residue 158
type
sequence M
description BINDING SITE FOR RESIDUE SF4 C 501
source : AC3

24) chain C
residue 158
type
sequence M
description BINDING SITE FOR RESIDUE SF4 D 501
source : AC4

25) chain D
residue 297
type
sequence C
description BINDING SITE FOR RESIDUE SF4 D 501
source : AC4

26) chain D
residue 298
type
sequence P
description BINDING SITE FOR RESIDUE SF4 D 501
source : AC4

27) chain D
residue 299
type
sequence G
description BINDING SITE FOR RESIDUE SF4 D 501
source : AC4

28) chain D
residue 300
type
sequence C
description BINDING SITE FOR RESIDUE SF4 D 501
source : AC4

29) chain D
residue 342
type
sequence G
description BINDING SITE FOR RESIDUE SF4 D 501
source : AC4

30) chain D
residue 343
type
sequence C
description BINDING SITE FOR RESIDUE SF4 D 501
source : AC4

31) chain D
residue 346
type
sequence N
description BINDING SITE FOR RESIDUE SF4 D 501
source : AC4

32) chain D
residue 350
type
sequence E
description BINDING SITE FOR RESIDUE SF4 D 501
source : AC4

33) chain A
residue 297
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158
source Swiss-Prot : SWS_FT_FI1

34) chain C
residue 300
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158
source Swiss-Prot : SWS_FT_FI1

35) chain C
residue 343
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158
source Swiss-Prot : SWS_FT_FI1

36) chain C
residue 350
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158
source Swiss-Prot : SWS_FT_FI1

37) chain D
residue 297
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158
source Swiss-Prot : SWS_FT_FI1

38) chain D
residue 300
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158
source Swiss-Prot : SWS_FT_FI1

39) chain D
residue 343
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158
source Swiss-Prot : SWS_FT_FI1

40) chain D
residue 350
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158
source Swiss-Prot : SWS_FT_FI1

41) chain A
residue 300
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158
source Swiss-Prot : SWS_FT_FI1

42) chain A
residue 343
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158
source Swiss-Prot : SWS_FT_FI1

43) chain A
residue 350
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158
source Swiss-Prot : SWS_FT_FI1

44) chain B
residue 297
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158
source Swiss-Prot : SWS_FT_FI1

45) chain B
residue 300
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158
source Swiss-Prot : SWS_FT_FI1

46) chain B
residue 343
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158
source Swiss-Prot : SWS_FT_FI1

47) chain B
residue 350
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158
source Swiss-Prot : SWS_FT_FI1

48) chain C
residue 297
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:21167158
source Swiss-Prot : SWS_FT_FI1


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