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

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Title Crystal Structure of the Exocytosis-Sensitive Phosphoprotein, pp63/Parafusin (phosphoglucomutase) from Paramecium
Classification ISOMERASE
Compound phosphoglucomutase 1
Source Paramecium tetraurelia (PARF_PARTE)
Sequence A:  QVIPAPRVQVTQPYAGQKPGTSGLRKKVSEATQPNYLENF
VQSIFNTLRKDELKPKNVLFVGGDGRYFNRQAIFSIIRLA
YANDISEVHVGQAGLMSTPASSHYIRKVNEEVGNCIGGII
LTASHNPGGKEHGDFGIKFNVRTGAPAPEDFTDQIYTHTT
KIKEYLTVDYEFEKHINLDQIGVYKFEGTRLEKSHFEVKV
VDTVQDYTQLMQKLFDFDLLKGLFSNKDFSFRFDGMHGVA
GPYAKHIFGTLLGCSKESLLNCDPSEDFGGGHPDPNLTYA
HDLVELLDIHKKKDVGTVPQFGAACDGDADRNMILGRQFF
VTPSDSLAVIAANANLIFKNGLLGAARSMPTSGALDKVAA
KNGIKLFETPTGWKFFGNLMDAGLINLCGEESFGTGSNHI
REKDGIWAVLAWLTILAHKNKNTDHFVTVEEIVTQYWQQF
GRNYYSRYDYEQVDSAGANKMMEHLKTKFQYFEQLKQGNK
ADIYDYVDPVDQSVSKNQGVRFVFGDGSRIIFRLSGTGSV
GATIRIYFEQFEQQQIQHETATALANIIKLGLEISDIAQF
TGRNEPTVIT
B:  QVIPAPRVQVTQPYAGQKPGTSGLRKKVSEATQPNYLENF
VQSIFNTLRKDELKPKNVLFVGGDGRYFNRQAIFSIIRLA
YANDISEVHVGQAGLMSTPASSHYIRKVNEEVGNCIGGII
LTASHNPGGKEHGDFGIKFNVRTGAPAPEDFTDQIYTHTT
KIKEYLTVDYEFEKHINLDQIGVYKFEGTRLEKSHFEVKV
VDTVQDYTQLMQKLFDFDLLKGLFSNKDFSFRFDGMHGVA
GPYAKHIFGTLLGCSKESLLNCDPSEDFGGGHPDPNLTYA
HDLVELLDIHKKKDVGTVPQFGAACDGDADRNMILGRQFF
VTPSDSLAVIAANANLIFKNGLLGAARSMPTSGALDKVAA
KNGIKLFETPTGWKFFGNLMDAGLINLCGEESFGTGSNHI
REKDGIWAVLAWLTILAHKNKNTDHFVTVEEIVTQYWQQF
GRNYYSRYDYEQVDSAGANKMMEHLKTKFQYFEQLKQGNK
ADIYDYVDPVDQSVSKNQGVRFVFGDGSRIIFRLSGTGSV
GATIRIYFEQFEQQQIQHETATALANIIKLGLEISDIAQF
TGRNEPTVIT
Description


Functional site

1) chain A
residue 308
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 700
source : AC1

2) chain A
residue 310
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 700
source : AC1

3) chain A
residue 312
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 700
source : AC1

4) chain A
residue 126
type
sequence S
description BINDING SITE FOR RESIDUE SO4 A 601
source : AC2

5) chain A
residue 127
type
sequence H
description BINDING SITE FOR RESIDUE SO4 A 601
source : AC2

6) chain A
residue 308
type
sequence D
description BINDING SITE FOR RESIDUE SO4 A 601
source : AC2

7) chain A
residue 310
type
sequence D
description BINDING SITE FOR RESIDUE SO4 A 601
source : AC2

8) chain A
residue 312
type
sequence D
description BINDING SITE FOR RESIDUE SO4 A 601
source : AC2

9) chain A
residue 313
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A 601
source : AC2

10) chain A
residue 405
type
sequence K
description BINDING SITE FOR RESIDUE SO4 A 601
source : AC2

11) chain A
residue 23
type
sequence T
description BINDING SITE FOR RESIDUE SO4 A 603
source : AC3

12) chain A
residue 515
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A 603
source : AC3

13) chain A
residue 517
type
sequence S
description BINDING SITE FOR RESIDUE SO4 A 603
source : AC3

14) chain A
residue 518
type
sequence G
description BINDING SITE FOR RESIDUE SO4 A 603
source : AC3

15) chain A
residue 519
type
sequence T
description BINDING SITE FOR RESIDUE SO4 A 603
source : AC3

16) chain A
residue 527
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A 603
source : AC3

17) chain B
residue 308
type
sequence D
description BINDING SITE FOR RESIDUE ZN B 700
source : AC4

18) chain B
residue 310
type
sequence D
description BINDING SITE FOR RESIDUE ZN B 700
source : AC4

19) chain B
residue 312
type
sequence D
description BINDING SITE FOR RESIDUE ZN B 700
source : AC4

20) chain B
residue 126
type
sequence S
description BINDING SITE FOR RESIDUE SO4 B 602
source : AC5

21) chain B
residue 127
type
sequence H
description BINDING SITE FOR RESIDUE SO4 B 602
source : AC5

22) chain B
residue 308
type
sequence D
description BINDING SITE FOR RESIDUE SO4 B 602
source : AC5

23) chain B
residue 312
type
sequence D
description BINDING SITE FOR RESIDUE SO4 B 602
source : AC5

24) chain B
residue 313
type
sequence R
description BINDING SITE FOR RESIDUE SO4 B 602
source : AC5

25) chain B
residue 375
type
sequence W
description BINDING SITE FOR RESIDUE SO4 B 602
source : AC5

26) chain B
residue 515
type
sequence R
description BINDING SITE FOR RESIDUE SO4 B 604
source : AC6

27) chain B
residue 517
type
sequence S
description BINDING SITE FOR RESIDUE SO4 B 604
source : AC6

28) chain B
residue 518
type
sequence G
description BINDING SITE FOR RESIDUE SO4 B 604
source : AC6

29) chain B
residue 519
type
sequence T
description BINDING SITE FOR RESIDUE SO4 B 604
source : AC6

30) chain B
residue 527
type
sequence R
description BINDING SITE FOR RESIDUE SO4 B 604
source : AC6

31) chain A
residue 120-129
type prosite
sequence GIILTASHNP
description PGM_PMM Phosphoglucomutase and phosphomannomutase phosphoserine signature. GIiLTASHNP
source prosite : PS00710

32) chain A
residue 126
type ACT_SITE
sequence S
description Phosphoserine intermediate
source Swiss-Prot : SWS_FT_FI1

33) chain B
residue 126
type ACT_SITE
sequence S
description Phosphoserine intermediate
source Swiss-Prot : SWS_FT_FI1

34) chain A
residue 23
type BINDING
sequence T
description BINDING => ECO:0000250|UniProtKB:P00949
source Swiss-Prot : SWS_FT_FI2

35) chain B
residue 140
type BINDING
sequence K
description BINDING => ECO:0000250|UniProtKB:P00949
source Swiss-Prot : SWS_FT_FI2

36) chain B
residue 373
type BINDING
sequence T
description BINDING => ECO:0000250|UniProtKB:P00949
source Swiss-Prot : SWS_FT_FI2

37) chain B
residue 392
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P00949
source Swiss-Prot : SWS_FT_FI2

38) chain B
residue 405
type BINDING
sequence K
description BINDING => ECO:0000250|UniProtKB:P00949
source Swiss-Prot : SWS_FT_FI2

39) chain B
residue 527
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P00949
source Swiss-Prot : SWS_FT_FI2

40) chain A
residue 27
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P00949
source Swiss-Prot : SWS_FT_FI2

41) chain A
residue 140
type BINDING
sequence K
description BINDING => ECO:0000250|UniProtKB:P00949
source Swiss-Prot : SWS_FT_FI2

42) chain A
residue 373
type BINDING
sequence T
description BINDING => ECO:0000250|UniProtKB:P00949
source Swiss-Prot : SWS_FT_FI2

43) chain A
residue 392
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P00949
source Swiss-Prot : SWS_FT_FI2

44) chain A
residue 405
type BINDING
sequence K
description BINDING => ECO:0000250|UniProtKB:P00949
source Swiss-Prot : SWS_FT_FI2

45) chain A
residue 527
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P00949
source Swiss-Prot : SWS_FT_FI2

46) chain B
residue 23
type BINDING
sequence T
description BINDING => ECO:0000250|UniProtKB:P00949
source Swiss-Prot : SWS_FT_FI2

47) chain B
residue 27
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P00949
source Swiss-Prot : SWS_FT_FI2

48) chain A
residue 126
type BINDING
sequence S
description via phosphate group
source Swiss-Prot : SWS_FT_FI3

49) chain B
residue 126
type BINDING
sequence S
description via phosphate group
source Swiss-Prot : SWS_FT_FI3

50) chain A
residue 308
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI4

51) chain A
residue 310
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI4

52) chain A
residue 312
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI4

53) chain B
residue 308
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI4

54) chain B
residue 310
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI4

55) chain B
residue 312
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI4


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