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

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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 C:  MIIVTGGAGFIGSNIVKALNDKGITDILVVDNLKDGTKFV
NLVDLNIADYMDKEDFLIQIMAGEEFGDVEAIFHEGAXSS
TTEWDGKYMMDNNYQYSKELLHYCLEREIPFLYASSAATY
GGRTSDFIESREYEKPLNVYGYSKFLFDEYVRQILPEANS
QIVGFRYFNVYGPREGHKGSMASVAFHLNTQLNFKRDFVY
VGDVADVNLWFLENGVSGIFNLGTGRAESFQAVADAYQAF
TQADLTNLRAAGYDKPFKTVAEGVTEYMAWLN
Description


Functional site

1) chain C
residue 6
type
sequence G
description BINDING SITE FOR RESIDUE NAP C 2402
source : AC5

2) chain C
residue 9
type
sequence G
description BINDING SITE FOR RESIDUE NAP C 2402
source : AC5

3) chain C
residue 10
type
sequence F
description BINDING SITE FOR RESIDUE NAP C 2402
source : AC5

4) chain C
residue 11
type
sequence I
description BINDING SITE FOR RESIDUE NAP C 2402
source : AC5

5) chain C
residue 31
type
sequence D
description BINDING SITE FOR RESIDUE NAP C 2402
source : AC5

6) chain C
residue 32
type
sequence N
description BINDING SITE FOR RESIDUE NAP C 2402
source : AC5

7) chain C
residue 38
type
sequence K
description BINDING SITE FOR RESIDUE NAP C 2402
source : AC5

8) chain C
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE NAP C 2402
source : AC5

9) chain C
residue 75
type
sequence E
description BINDING SITE FOR RESIDUE NAP C 2402
source : AC5

10) chain C
residue 76
type
sequence G
description BINDING SITE FOR RESIDUE NAP C 2402
source : AC5

11) chain C
residue 77
type
sequence A
description BINDING SITE FOR RESIDUE NAP C 2402
source : AC5

12) chain C
residue 79
type
sequence S
description BINDING SITE FOR RESIDUE NAP C 2402
source : AC5

13) chain C
residue 92
type
sequence N
description BINDING SITE FOR RESIDUE NAP C 2402
source : AC5

14) chain C
residue 96
type
sequence Y
description BINDING SITE FOR RESIDUE NAP C 2402
source : AC5

15) chain C
residue 114
type
sequence A
description BINDING SITE FOR RESIDUE NAP C 2402
source : AC5

16) chain C
residue 115
type
sequence S
description BINDING SITE FOR RESIDUE NAP C 2402
source : AC5

17) chain C
residue 116
type
sequence S
description BINDING SITE FOR RESIDUE NAP C 2402
source : AC5

18) chain C
residue 140
type
sequence Y
description BINDING SITE FOR RESIDUE NAP C 2402
source : AC5

19) chain C
residue 144
type
sequence K
description BINDING SITE FOR RESIDUE NAP C 2402
source : AC5

20) chain C
residue 167
type
sequence Y
description BINDING SITE FOR RESIDUE NAP C 2402
source : AC5

21) chain C
residue 168
type
sequence F
description BINDING SITE FOR RESIDUE NAP C 2402
source : AC5

22) chain C
residue 170
type
sequence V
description BINDING SITE FOR RESIDUE NAP C 2402
source : AC5

23) chain C
residue 177
type
sequence H
description BINDING SITE FOR RESIDUE NAP C 2402
source : AC5

24) chain C
residue 178
type
sequence K
description BINDING SITE FOR RESIDUE NAP C 2402
source : AC5

25) chain C
residue 81
type
sequence T
description BINDING SITE FOR RESIDUE ADQ C 2502
source : AC6

26) chain C
residue 169
type
sequence N
description BINDING SITE FOR RESIDUE ADQ C 2502
source : AC6

27) chain C
residue 180
type
sequence S
description BINDING SITE FOR RESIDUE ADQ C 2502
source : AC6

28) chain C
residue 181
type
sequence M
description BINDING SITE FOR RESIDUE ADQ C 2502
source : AC6

29) chain C
residue 182
type
sequence A
description BINDING SITE FOR RESIDUE ADQ C 2502
source : AC6

30) chain C
residue 184
type
sequence V
description BINDING SITE FOR RESIDUE ADQ C 2502
source : AC6

31) chain C
residue 187
type
sequence H
description BINDING SITE FOR RESIDUE ADQ C 2502
source : AC6

32) chain C
residue 209
type
sequence R
description BINDING SITE FOR RESIDUE ADQ C 2502
source : AC6

33) chain C
residue 243
type
sequence F
description BINDING SITE FOR RESIDUE ADQ C 2502
source : AC6

34) chain C
residue 272
type
sequence Y
description BINDING SITE FOR RESIDUE ADQ C 2502
source : AC6

35) chain C
residue 116
type catalytic
sequence S
description 557
source MCSA : MCSA3

36) chain C
residue 140
type catalytic
sequence Y
description 557
source MCSA : MCSA3

37) chain C
residue 178
type catalytic
sequence K
description 557
source MCSA : MCSA3

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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


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