eF-site ID 1eq2-F
PDB Code 1eq2
Chain F

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Title THE CRYSTAL STRUCTURE OF ADP-L-GLYCERO-D-MANNOHEPTOSE 6-EPIMERASE
Classification ISOMERASE
Compound ADP-L-GLYCERO-D-MANNOHEPTOSE 6-EPIMERASE
Source Escherichia coli (strain K12) (HLDD_ECOLI)
Sequence F:  MIIVTGGAGFIGSNIVKALNDKGITDILVVDNLKDGTKFV
NLVDLNIADYMDKEDFLIQIMAGEEFGDVEAIFHEGAXSS
TTEWDGKYMMDNNYQYSKELLHYCLEREIPFLYASSAATY
GGRTSDFIESREYEKPLNVYGYSKFLFDEYVRQILPEANS
QIVGFRYFNVYGPREGHKGSMASVAFHLNTQLNNGESPKL
FEGSENFKRDFVYVGDVADVNLWFLENGVSGIFNLGTGRA
ESFQAVADATLAYHKKGQIEYIPFPDKLKGRYQAFTQADL
TNLRAAGYDKPFKTVAEGVTEYMAWLN
Description


Functional site

1) chain F
residue 6
type
sequence G
description BINDING SITE FOR RESIDUE NAP F 2405
source : BC2

2) chain F
residue 9
type
sequence G
description BINDING SITE FOR RESIDUE NAP F 2405
source : BC2

3) chain F
residue 10
type
sequence F
description BINDING SITE FOR RESIDUE NAP F 2405
source : BC2

4) chain F
residue 11
type
sequence I
description BINDING SITE FOR RESIDUE NAP F 2405
source : BC2

5) chain F
residue 31
type
sequence D
description BINDING SITE FOR RESIDUE NAP F 2405
source : BC2

6) chain F
residue 32
type
sequence N
description BINDING SITE FOR RESIDUE NAP F 2405
source : BC2

7) chain F
residue 38
type
sequence K
description BINDING SITE FOR RESIDUE NAP F 2405
source : BC2

8) chain F
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE NAP F 2405
source : BC2

9) chain F
residue 75
type
sequence E
description BINDING SITE FOR RESIDUE NAP F 2405
source : BC2

10) chain F
residue 76
type
sequence G
description BINDING SITE FOR RESIDUE NAP F 2405
source : BC2

11) chain F
residue 77
type
sequence A
description BINDING SITE FOR RESIDUE NAP F 2405
source : BC2

12) chain F
residue 79
type
sequence S
description BINDING SITE FOR RESIDUE NAP F 2405
source : BC2

13) chain F
residue 92
type
sequence N
description BINDING SITE FOR RESIDUE NAP F 2405
source : BC2

14) chain F
residue 96
type
sequence Y
description BINDING SITE FOR RESIDUE NAP F 2405
source : BC2

15) chain F
residue 114
type
sequence A
description BINDING SITE FOR RESIDUE NAP F 2405
source : BC2

16) chain F
residue 115
type
sequence S
description BINDING SITE FOR RESIDUE NAP F 2405
source : BC2

17) chain F
residue 116
type
sequence S
description BINDING SITE FOR RESIDUE NAP F 2405
source : BC2

18) chain F
residue 140
type
sequence Y
description BINDING SITE FOR RESIDUE NAP F 2405
source : BC2

19) chain F
residue 144
type
sequence K
description BINDING SITE FOR RESIDUE NAP F 2405
source : BC2

20) chain F
residue 167
type
sequence Y
description BINDING SITE FOR RESIDUE NAP F 2405
source : BC2

21) chain F
residue 168
type
sequence F
description BINDING SITE FOR RESIDUE NAP F 2405
source : BC2

22) chain F
residue 170
type
sequence V
description BINDING SITE FOR RESIDUE NAP F 2405
source : BC2

23) chain F
residue 177
type
sequence H
description BINDING SITE FOR RESIDUE NAP F 2405
source : BC2

24) chain F
residue 178
type
sequence K
description BINDING SITE FOR RESIDUE NAP F 2405
source : BC2

25) chain F
residue 117
type
sequence A
description BINDING SITE FOR RESIDUE ADQ F 2505
source : BC3

26) chain F
residue 167
type
sequence Y
description BINDING SITE FOR RESIDUE ADQ F 2505
source : BC3

27) chain F
residue 168
type
sequence F
description BINDING SITE FOR RESIDUE ADQ F 2505
source : BC3

28) chain F
residue 169
type
sequence N
description BINDING SITE FOR RESIDUE ADQ F 2505
source : BC3

29) chain F
residue 180
type
sequence S
description BINDING SITE FOR RESIDUE ADQ F 2505
source : BC3

30) chain F
residue 182
type
sequence A
description BINDING SITE FOR RESIDUE ADQ F 2505
source : BC3

31) chain F
residue 187
type
sequence H
description BINDING SITE FOR RESIDUE ADQ F 2505
source : BC3

32) chain F
residue 200
type
sequence L
description BINDING SITE FOR RESIDUE ADQ F 2505
source : BC3

33) chain F
residue 201
type
sequence F
description BINDING SITE FOR RESIDUE ADQ F 2505
source : BC3

34) chain F
residue 204
type
sequence S
description BINDING SITE FOR RESIDUE ADQ F 2505
source : BC3

35) chain F
residue 209
type
sequence R
description BINDING SITE FOR RESIDUE ADQ F 2505
source : BC3

36) chain F
residue 243
type
sequence F
description BINDING SITE FOR RESIDUE ADQ F 2505
source : BC3

37) chain F
residue 268
type
sequence L
description BINDING SITE FOR RESIDUE ADQ F 2505
source : BC3

38) chain F
residue 272
type
sequence Y
description BINDING SITE FOR RESIDUE ADQ F 2505
source : BC3

39) chain F
residue 273
type
sequence Q
description BINDING SITE FOR RESIDUE ADQ F 2505
source : BC3

40) chain F
residue 276
type
sequence T
description BINDING SITE FOR RESIDUE ADQ F 2505
source : BC3

41) chain F
residue 116
type catalytic
sequence S
description 557
source MCSA : MCSA6

42) chain F
residue 140
type catalytic
sequence Y
description 557
source MCSA : MCSA6

43) chain F
residue 178
type catalytic
sequence K
description 557
source MCSA : MCSA6

44) chain F
residue 140
type ACT_SITE
sequence Y
description Proton acceptor => ECO:0000269|PubMed:17316025
source Swiss-Prot : SWS_FT_FI1

45) chain F
residue 178
type ACT_SITE
sequence K
description Proton acceptor => ECO:0000269|PubMed:17316025
source Swiss-Prot : SWS_FT_FI1

46) chain F
residue 10
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:10896473
source Swiss-Prot : SWS_FT_FI2

47) chain F
residue 31
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:10896473
source Swiss-Prot : SWS_FT_FI2

48) chain F
residue 38
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:10896473
source Swiss-Prot : SWS_FT_FI2

49) chain F
residue 53
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:10896473
source Swiss-Prot : SWS_FT_FI2

50) chain F
residue 75
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10896473
source Swiss-Prot : SWS_FT_FI2

51) chain F
residue 92
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:10896473
source Swiss-Prot : SWS_FT_FI2

52) chain F
residue 144
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:10896473
source Swiss-Prot : SWS_FT_FI2

53) chain F
residue 169
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:10896473
source Swiss-Prot : SWS_FT_FI2

54) chain F
residue 170
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:10896473
source Swiss-Prot : SWS_FT_FI2

55) chain F
residue 178
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:10896473
source Swiss-Prot : SWS_FT_FI2

56) chain F
residue 180
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:10896473
source Swiss-Prot : SWS_FT_FI2

57) chain F
residue 187
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:10896473
source Swiss-Prot : SWS_FT_FI2

58) chain F
residue 201
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:10896473
source Swiss-Prot : SWS_FT_FI2

59) chain F
residue 209
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:10896473
source Swiss-Prot : SWS_FT_FI2

60) chain F
residue 272
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:10896473
source Swiss-Prot : SWS_FT_FI2

61) chain F
residue 267
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:18723842
source Swiss-Prot : SWS_FT_FI3


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