eF-site ID 1x9i-AB
PDB Code 1x9i
Chain A, B

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Title Crystal structure of Crystal structure of phosphoglucose/phosphomannose phosphoglucose/phosphomannoseisomerase from Pyrobaculum aerophilum in complex with glucose 6-phosphate
Classification ISOMERASE
Compound glucose-6-phosphate isomerase
Source (NP_559417)
Sequence A:  SQLLQDYLNWENYILRRVDFPTSYVVEGEVVRIEAMPRLY
ISGMGGSGVVADLIRDFSLTWNWEVEVIAVKDYFLKARDG
LLIAVSYSGNTIETLYTVEYAKRRRIPAVAITTGGRLAQM
GVPTVIVPKASAPRAALPQLLTAALHVVAKVYGIDVKIPE
GLEPPNEALIHKLVEEFQKRPTIIAAESMRGVAYRVKNEF
NENAKIEPSVEILPEAHHNWIEGSERAVVALTSPHIPKEH
QERVKATVEIVGGSIYAVEMHPKGVLSFLRDVGIASVKLA
EIRGVNPLATPRIDALKRRL
B:  SQLLQDYLNWENYILRRVDFPTSYVVEGEVVRIEAMPRLY
ISGMGGSGVVADLIRDFSLTWNWEVEVIAVKDYFLKARDG
LLIAVSYSGNTIETLYTVEYAKRRRIPAVAITTGGRLAQM
GVPTVIVPKASAPRAALPQLLTAALHVVAKVYGIDVKIPE
GLEPPNEALIHKLVEEFQKRPTIIAAESMRGVAYRVKNEF
NENAKIEPSVEILPEAHHNWIEGSERAVVALTSPHIPKEH
QERVKATVEIVGGSIYAVEMHPKGVLSFLRDVGIASVKLA
EIRGVNPLATPRIDALKRRLQ
Description


Functional site

1) chain A
residue 45
type
sequence M
description BINDING SITE FOR RESIDUE G6Q A 600
source : AC1

2) chain A
residue 46
type
sequence G
description BINDING SITE FOR RESIDUE G6Q A 600
source : AC1

3) chain A
residue 47
type
sequence G
description BINDING SITE FOR RESIDUE G6Q A 600
source : AC1

4) chain A
residue 48
type
sequence S
description BINDING SITE FOR RESIDUE G6Q A 600
source : AC1

5) chain A
residue 87
type
sequence S
description BINDING SITE FOR RESIDUE G6Q A 600
source : AC1

6) chain A
residue 88
type
sequence Y
description BINDING SITE FOR RESIDUE G6Q A 600
source : AC1

7) chain A
residue 89
type
sequence S
description BINDING SITE FOR RESIDUE G6Q A 600
source : AC1

8) chain A
residue 92
type
sequence T
description BINDING SITE FOR RESIDUE G6Q A 600
source : AC1

9) chain A
residue 134
type
sequence P
description BINDING SITE FOR RESIDUE G6Q A 600
source : AC1

10) chain A
residue 135
type
sequence R
description BINDING SITE FOR RESIDUE G6Q A 600
source : AC1

11) chain A
residue 203
type
sequence E
description BINDING SITE FOR RESIDUE G6Q A 600
source : AC1

12) chain A
residue 298
type
sequence K
description BINDING SITE FOR RESIDUE G6Q A 600
source : AC1

13) chain B
residue 219
type
sequence H
description BINDING SITE FOR RESIDUE G6Q A 600
source : AC1

14) chain A
residue 219
type
sequence H
description BINDING SITE FOR RESIDUE G6Q B 601
source : AC2

15) chain B
residue 45
type
sequence M
description BINDING SITE FOR RESIDUE G6Q B 601
source : AC2

16) chain B
residue 46
type
sequence G
description BINDING SITE FOR RESIDUE G6Q B 601
source : AC2

17) chain B
residue 47
type
sequence G
description BINDING SITE FOR RESIDUE G6Q B 601
source : AC2

18) chain B
residue 48
type
sequence S
description BINDING SITE FOR RESIDUE G6Q B 601
source : AC2

19) chain B
residue 87
type
sequence S
description BINDING SITE FOR RESIDUE G6Q B 601
source : AC2

20) chain B
residue 88
type
sequence Y
description BINDING SITE FOR RESIDUE G6Q B 601
source : AC2

21) chain B
residue 89
type
sequence S
description BINDING SITE FOR RESIDUE G6Q B 601
source : AC2

22) chain B
residue 92
type
sequence T
description BINDING SITE FOR RESIDUE G6Q B 601
source : AC2

23) chain B
residue 134
type
sequence P
description BINDING SITE FOR RESIDUE G6Q B 601
source : AC2

24) chain B
residue 135
type
sequence R
description BINDING SITE FOR RESIDUE G6Q B 601
source : AC2

25) chain B
residue 203
type
sequence E
description BINDING SITE FOR RESIDUE G6Q B 601
source : AC2

26) chain B
residue 298
type
sequence K
description BINDING SITE FOR RESIDUE G6Q B 601
source : AC2

27) chain A
residue 53
type
sequence D
description BINDING SITE FOR RESIDUE GOL A 701
source : AC3

28) chain A
residue 72
type
sequence K
description BINDING SITE FOR RESIDUE GOL A 701
source : AC3

29) chain A
residue 191
type
sequence R
description BINDING SITE FOR RESIDUE GOL A 701
source : AC3

30) chain A
residue 195
type
sequence Y
description BINDING SITE FOR RESIDUE GOL A 701
source : AC3

31) chain A
residue 70
type
sequence A
description BINDING SITE FOR RESIDUE GOL A 702
source : AC4

32) chain A
residue 71
type
sequence V
description BINDING SITE FOR RESIDUE GOL A 702
source : AC4

33) chain A
residue 72
type
sequence K
description BINDING SITE FOR RESIDUE GOL A 702
source : AC4

34) chain A
residue 73
type
sequence D
description BINDING SITE FOR RESIDUE GOL A 702
source : AC4

35) chain B
residue 56
type
sequence R
description BINDING SITE FOR RESIDUE GOL A 702
source : AC4

36) chain B
residue 188
type
sequence E
description BINDING SITE FOR RESIDUE GOL A 702
source : AC4

37) chain A
residue 135
type catalytic
sequence R
description 736
source MCSA : MCSA1

38) chain A
residue 203
type catalytic
sequence E
description 736
source MCSA : MCSA1

39) chain A
residue 219
type catalytic
sequence H
description 736
source MCSA : MCSA1

40) chain A
residue 298
type catalytic
sequence K
description 736
source MCSA : MCSA1

41) chain B
residue 135
type catalytic
sequence R
description 736
source MCSA : MCSA2

42) chain B
residue 203
type catalytic
sequence E
description 736
source MCSA : MCSA2

43) chain B
residue 219
type catalytic
sequence H
description 736
source MCSA : MCSA2

44) chain B
residue 298
type catalytic
sequence K
description 736
source MCSA : MCSA2

45) chain A
residue 48
type BINDING
sequence S
description
source Swiss-Prot : SWS_FT_FI3

46) chain A
residue 87
type BINDING
sequence S
description
source Swiss-Prot : SWS_FT_FI3

47) chain A
residue 92
type BINDING
sequence T
description
source Swiss-Prot : SWS_FT_FI3

48) chain B
residue 48
type BINDING
sequence S
description
source Swiss-Prot : SWS_FT_FI3

49) chain B
residue 87
type BINDING
sequence S
description
source Swiss-Prot : SWS_FT_FI3

50) chain B
residue 92
type BINDING
sequence T
description
source Swiss-Prot : SWS_FT_FI3

51) chain A
residue 203
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000305
source Swiss-Prot : SWS_FT_FI1

52) chain A
residue 298
type ACT_SITE
sequence K
description Proton acceptor => ECO:0000305
source Swiss-Prot : SWS_FT_FI1

53) chain B
residue 203
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000305
source Swiss-Prot : SWS_FT_FI1

54) chain B
residue 298
type ACT_SITE
sequence K
description Proton acceptor => ECO:0000305
source Swiss-Prot : SWS_FT_FI1

55) chain A
residue 219
type ACT_SITE
sequence H
description Proton donor => ECO:0000305
source Swiss-Prot : SWS_FT_FI2

56) chain B
residue 219
type ACT_SITE
sequence H
description Proton donor => ECO:0000305
source Swiss-Prot : SWS_FT_FI2


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