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

click to enlarge
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 A:  MIIVTGGAGFIGSNIVKALNDKGITDILVVDNLKDGTKFV
NLVDLNIADYMDKEDFLIQIMAGEEFGDVEAIFHEGAXSS
TTEWDGKYMMDNNYQYSKELLHYCLEREIPFLYASSAATY
GGRTSDFIESREYEKPLNVYGYSKFLFDEYVRQILPEANS
QIVGFRYFNVYGPREGHKGSMASVAFHLNTQLNNKRDFVY
VGDVADVNLWFLENGVSGIFNLGTGRAESFQAVADATYQA
FTQADLTNLRAAGYDKPFKTVAEGVTEYMAWLN
Description


Functional site

1) chain A
residue 6
type
sequence G
description BINDING SITE FOR RESIDUE NAP A 2400
source : AC1

2) chain A
residue 9
type
sequence G
description BINDING SITE FOR RESIDUE NAP A 2400
source : AC1

3) chain A
residue 10
type
sequence F
description BINDING SITE FOR RESIDUE NAP A 2400
source : AC1

4) chain A
residue 11
type
sequence I
description BINDING SITE FOR RESIDUE NAP A 2400
source : AC1

5) chain A
residue 31
type
sequence D
description BINDING SITE FOR RESIDUE NAP A 2400
source : AC1

6) chain A
residue 32
type
sequence N
description BINDING SITE FOR RESIDUE NAP A 2400
source : AC1

7) chain A
residue 38
type
sequence K
description BINDING SITE FOR RESIDUE NAP A 2400
source : AC1

8) chain A
residue 53
type
sequence K
description BINDING SITE FOR RESIDUE NAP A 2400
source : AC1

9) chain A
residue 75
type
sequence E
description BINDING SITE FOR RESIDUE NAP A 2400
source : AC1

10) chain A
residue 76
type
sequence G
description BINDING SITE FOR RESIDUE NAP A 2400
source : AC1

11) chain A
residue 77
type
sequence A
description BINDING SITE FOR RESIDUE NAP A 2400
source : AC1

12) chain A
residue 79
type
sequence S
description BINDING SITE FOR RESIDUE NAP A 2400
source : AC1

13) chain A
residue 92
type
sequence N
description BINDING SITE FOR RESIDUE NAP A 2400
source : AC1

14) chain A
residue 96
type
sequence Y
description BINDING SITE FOR RESIDUE NAP A 2400
source : AC1

15) chain A
residue 114
type
sequence A
description BINDING SITE FOR RESIDUE NAP A 2400
source : AC1

16) chain A
residue 115
type
sequence S
description BINDING SITE FOR RESIDUE NAP A 2400
source : AC1

17) chain A
residue 116
type
sequence S
description BINDING SITE FOR RESIDUE NAP A 2400
source : AC1

18) chain A
residue 140
type
sequence Y
description BINDING SITE FOR RESIDUE NAP A 2400
source : AC1

19) chain A
residue 144
type
sequence K
description BINDING SITE FOR RESIDUE NAP A 2400
source : AC1

20) chain A
residue 167
type
sequence Y
description BINDING SITE FOR RESIDUE NAP A 2400
source : AC1

21) chain A
residue 168
type
sequence F
description BINDING SITE FOR RESIDUE NAP A 2400
source : AC1

22) chain A
residue 170
type
sequence V
description BINDING SITE FOR RESIDUE NAP A 2400
source : AC1

23) chain A
residue 177
type
sequence H
description BINDING SITE FOR RESIDUE NAP A 2400
source : AC1

24) chain A
residue 178
type
sequence K
description BINDING SITE FOR RESIDUE NAP A 2400
source : AC1

25) chain A
residue 81
type
sequence T
description BINDING SITE FOR RESIDUE ADQ A 2500
source : AC2

26) chain A
residue 169
type
sequence N
description BINDING SITE FOR RESIDUE ADQ A 2500
source : AC2

27) chain A
residue 180
type
sequence S
description BINDING SITE FOR RESIDUE ADQ A 2500
source : AC2

28) chain A
residue 182
type
sequence A
description BINDING SITE FOR RESIDUE ADQ A 2500
source : AC2

29) chain A
residue 187
type
sequence H
description BINDING SITE FOR RESIDUE ADQ A 2500
source : AC2

30) chain A
residue 209
type
sequence R
description BINDING SITE FOR RESIDUE ADQ A 2500
source : AC2

31) chain A
residue 243
type
sequence F
description BINDING SITE FOR RESIDUE ADQ A 2500
source : AC2

32) chain A
residue 116
type catalytic
sequence S
description 557
source MCSA : MCSA1

33) chain A
residue 140
type catalytic
sequence Y
description 557
source MCSA : MCSA1

34) chain A
residue 178
type catalytic
sequence K
description 557
source MCSA : MCSA1

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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


Display surface

Download
Links