eF-site ID 1cde-BC
PDB Code 1cde
Chain B, C

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Title STRUCTURES OF APO AND COMPLEXED ESCHERICHIA COLI GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE
Classification TRANSFERASE(FORMYL)
Compound PHOSPHORIBOSYL-GLYCINAMIDE FORMYLTRANSFERASE
Source Escherichia coli (strain K12) (PUR3_ECOLI)
Sequence B:  MNIVVLISGNGSNLQAIIDACKTNKIKGTVRAVFSNKADA
FGLERARQAGIATHTLIASAFDSREAYDRELIHEIDMYAP
DVVVLAGFMRILSPAFVSHYAGRLLNIHPSLLPKYPGLHT
HRQALENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGD
SEDDITARVQTQEHAIYPLVISWFADGRLKMHENAAWLDG
QRLPPQGYA
C:  MNIVVLISGNGSNLQAIIDACKTNKIKGTVRAVFSNKADA
FGLERARQAGIATHTLIASAFDSREAYDRELIHEIDMYAP
DVVVLAGFMRILSPAFVSHYAGRLLNIHPSLLPKYPGLHT
HRQALENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGD
SEDDITARVQTQEHAIYPLVISWFADGRLKMHENAAWLDG
QRLPPQGYA
Description


Functional site

1) chain B
residue 10
type
sequence N
description BINDING SITE FOR RESIDUE GAR B 222
source : AC3

2) chain B
residue 11
type
sequence G
description BINDING SITE FOR RESIDUE GAR B 222
source : AC3

3) chain B
residue 12
type
sequence S
description BINDING SITE FOR RESIDUE GAR B 222
source : AC3

4) chain B
residue 13
type
sequence N
description BINDING SITE FOR RESIDUE GAR B 222
source : AC3

5) chain B
residue 87
type
sequence G
description BINDING SITE FOR RESIDUE GAR B 222
source : AC3

6) chain B
residue 89
type
sequence M
description BINDING SITE FOR RESIDUE GAR B 222
source : AC3

7) chain B
residue 107
type
sequence I
description BINDING SITE FOR RESIDUE GAR B 222
source : AC3

8) chain B
residue 108
type
sequence H
description BINDING SITE FOR RESIDUE GAR B 222
source : AC3

9) chain B
residue 109
type
sequence P
description BINDING SITE FOR RESIDUE GAR B 222
source : AC3

10) chain B
residue 170
type
sequence Q
description BINDING SITE FOR RESIDUE GAR B 222
source : AC3

11) chain B
residue 173
type
sequence E
description BINDING SITE FOR RESIDUE GAR B 222
source : AC3

12) chain B
residue 89
type
sequence M
description BINDING SITE FOR RESIDUE DZF B 225
source : AC4

13) chain B
residue 90
type
sequence R
description BINDING SITE FOR RESIDUE DZF B 225
source : AC4

14) chain B
residue 91
type
sequence I
description BINDING SITE FOR RESIDUE DZF B 225
source : AC4

15) chain B
residue 92
type
sequence L
description BINDING SITE FOR RESIDUE DZF B 225
source : AC4

16) chain B
residue 97
type
sequence V
description BINDING SITE FOR RESIDUE DZF B 225
source : AC4

17) chain B
residue 106
type
sequence N
description BINDING SITE FOR RESIDUE DZF B 225
source : AC4

18) chain B
residue 139
type
sequence V
description BINDING SITE FOR RESIDUE DZF B 225
source : AC4

19) chain B
residue 140
type
sequence T
description BINDING SITE FOR RESIDUE DZF B 225
source : AC4

20) chain B
residue 141
type
sequence D
description BINDING SITE FOR RESIDUE DZF B 225
source : AC4

21) chain B
residue 142
type
sequence E
description BINDING SITE FOR RESIDUE DZF B 225
source : AC4

22) chain B
residue 144
type
sequence D
description BINDING SITE FOR RESIDUE DZF B 225
source : AC4

23) chain C
residue 10
type
sequence N
description BINDING SITE FOR RESIDUE GAR C 222
source : AC5

24) chain C
residue 11
type
sequence G
description BINDING SITE FOR RESIDUE GAR C 222
source : AC5

25) chain C
residue 12
type
sequence S
description BINDING SITE FOR RESIDUE GAR C 222
source : AC5

26) chain C
residue 13
type
sequence N
description BINDING SITE FOR RESIDUE GAR C 222
source : AC5

27) chain C
residue 87
type
sequence G
description BINDING SITE FOR RESIDUE GAR C 222
source : AC5

28) chain C
residue 89
type
sequence M
description BINDING SITE FOR RESIDUE GAR C 222
source : AC5

29) chain C
residue 107
type
sequence I
description BINDING SITE FOR RESIDUE GAR C 222
source : AC5

30) chain C
residue 108
type
sequence H
description BINDING SITE FOR RESIDUE GAR C 222
source : AC5

31) chain C
residue 109
type
sequence P
description BINDING SITE FOR RESIDUE GAR C 222
source : AC5

32) chain C
residue 170
type
sequence Q
description BINDING SITE FOR RESIDUE GAR C 222
source : AC5

33) chain C
residue 173
type
sequence E
description BINDING SITE FOR RESIDUE GAR C 222
source : AC5

34) chain C
residue 89
type
sequence M
description BINDING SITE FOR RESIDUE DZF C 225
source : AC6

35) chain C
residue 90
type
sequence R
description BINDING SITE FOR RESIDUE DZF C 225
source : AC6

36) chain C
residue 91
type
sequence I
description BINDING SITE FOR RESIDUE DZF C 225
source : AC6

37) chain C
residue 92
type
sequence L
description BINDING SITE FOR RESIDUE DZF C 225
source : AC6

38) chain C
residue 97
type
sequence V
description BINDING SITE FOR RESIDUE DZF C 225
source : AC6

39) chain C
residue 106
type
sequence N
description BINDING SITE FOR RESIDUE DZF C 225
source : AC6

40) chain C
residue 139
type
sequence V
description BINDING SITE FOR RESIDUE DZF C 225
source : AC6

41) chain C
residue 140
type
sequence T
description BINDING SITE FOR RESIDUE DZF C 225
source : AC6

42) chain C
residue 141
type
sequence D
description BINDING SITE FOR RESIDUE DZF C 225
source : AC6

43) chain C
residue 142
type
sequence E
description BINDING SITE FOR RESIDUE DZF C 225
source : AC6

44) chain C
residue 144
type
sequence D
description BINDING SITE FOR RESIDUE DZF C 225
source : AC6

45) chain B
residue 11
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1631098
source Swiss-Prot : SWS_FT_FI2

46) chain B
residue 89
type BINDING
sequence M
description BINDING => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1631098
source Swiss-Prot : SWS_FT_FI2

47) chain C
residue 11
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1631098
source Swiss-Prot : SWS_FT_FI2

48) chain C
residue 89
type BINDING
sequence M
description BINDING => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1631098
source Swiss-Prot : SWS_FT_FI2

49) chain B
residue 64
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10606510
source Swiss-Prot : SWS_FT_FI3

50) chain B
residue 106
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10606510
source Swiss-Prot : SWS_FT_FI3

51) chain C
residue 64
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10606510
source Swiss-Prot : SWS_FT_FI3

52) chain C
residue 106
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10606510
source Swiss-Prot : SWS_FT_FI3

53) chain B
residue 108
type ACT_SITE
sequence H
description Proton donor => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10433709
source Swiss-Prot : SWS_FT_FI1

54) chain C
residue 108
type ACT_SITE
sequence H
description Proton donor => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10433709
source Swiss-Prot : SWS_FT_FI1

55) chain B
residue 106
type catalytic
sequence N
description 363
source MCSA : MCSA2

56) chain B
residue 108
type catalytic
sequence H
description 363
source MCSA : MCSA2

57) chain B
residue 135
type catalytic
sequence S
description 363
source MCSA : MCSA2

58) chain B
residue 144
type catalytic
sequence D
description 363
source MCSA : MCSA2

59) chain C
residue 106
type catalytic
sequence N
description 363
source MCSA : MCSA3

60) chain C
residue 108
type catalytic
sequence H
description 363
source MCSA : MCSA3

61) chain C
residue 135
type catalytic
sequence S
description 363
source MCSA : MCSA3

62) chain C
residue 144
type catalytic
sequence D
description 363
source MCSA : MCSA3

63) chain B
residue 140
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1631098
source Swiss-Prot : SWS_FT_FI4

64) chain B
residue 170
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1631098
source Swiss-Prot : SWS_FT_FI4

65) chain C
residue 140
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1631098
source Swiss-Prot : SWS_FT_FI4

66) chain C
residue 170
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1631098
source Swiss-Prot : SWS_FT_FI4

67) chain B
residue 144
type SITE
sequence D
description Raises pKa of active site His => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10433709
source Swiss-Prot : SWS_FT_FI5

68) chain C
residue 144
type SITE
sequence D
description Raises pKa of active site His => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10433709
source Swiss-Prot : SWS_FT_FI5


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