eF-site ID 3nd7-ABCDEF
PDB Code 3nd7
Chain A, B, C, D, E, F

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Title Crystal structure of phosphopantetheine adenylyltransferase from Enterococcus faecalis in the ligand-unbound state and in complex with ATP and pantetheine
Classification TRANSFERASE
Compound Phosphopantetheine adenylyltransferase
Source Enterococcus faecalis (Streptococcus faecalis) (COAD_ENTFA)
Sequence A:  MRKIALFPGSFDPMTNGHLNLIERSAKLFDEVIIGVFILF
TPEEKKYLIEEATKEMPNVRVIMQETQLTVESAKSLGANF
LIRGIRNVKDYEYEKDIAKMNQHLAPEIETVFLLAEEPYA
HVSSSLLKEVLRFGGDVSDYLPPNIYHALKQK
B:  MRKIALFPGSFDPMTNGHLNLIERSAKLFDEVIIGVFILF
TPEEKKYLIEEATKEMPNVRVIMQETQLTVESAKSLGANF
LIRGIRNVKDYEYEKDIAKMNQHLAPEIETVFLLAEEPYA
HVSSSLLKEVLRFGGDVSDYLPPNIYHALKQK
C:  MRKIALFPGSFDPMTNGHLNLIERSAKLFDEVIIGVFILF
TPEEKKYLIEEATKEMPNVRVIMQETQLTVESAKSLGANF
LIRGIRNVKDYEYEKDIAKMNQHLAPEIETVFLLAEEPYA
HVSSSLLKEVLRFGGDVSDYLPPNIYHALKQK
D:  MRKIALFPGSFDPMTNGHLNLIERSAKLFDEVIIGVFILF
TPEEKKYLIEEATKEMPNVRVIMQETQLTVESAKSLGANF
LIRGIRNVKDYEYEKDIAKMNQHLAPEIETVFLLAEEPYA
HVSSSLLKEVLRFGGDVSDYLPPNIYHALKQK
E:  MRKIALFPGSFDPMTNGHLNLIERSAKLFDEVIIGVFILF
TPEEKKYLIEEATKEMPNVRVIMQETQLTVESAKSLGANF
LIRGIRNVKDYEYEKDIAKMNQHLAPEIETVFLLAEEPYA
HVSSSLLKEVLRFGGDVSDYLPPNIYHALKQK
F:  MRKIALFPGSFDPMTNGHLNLIERSAKLFDEVIIGVFILF
TPEEKKYLIEEATKEMPNVRVIMQETQLTVESAKSLGANF
LIRGIRNVKDYEYEKDIAKMNQHLAPEIETVFLLAEEPYA
HVSSSLLKEVLRFGGDVSDYLPPNIYHALKQK
Description


Functional site

1) chain A
residue 9
type
sequence G
description BINDING SITE FOR RESIDUE PNY A 501
source : AC1

2) chain A
residue 10
type
sequence S
description BINDING SITE FOR RESIDUE PNY A 501
source : AC1

3) chain A
residue 73
type
sequence Q
description BINDING SITE FOR RESIDUE PNY A 501
source : AC1

4) chain A
residue 74
type
sequence L
description BINDING SITE FOR RESIDUE PNY A 501
source : AC1

5) chain A
residue 75
type
sequence T
description BINDING SITE FOR RESIDUE PNY A 501
source : AC1

6) chain A
residue 99
type
sequence Y
description BINDING SITE FOR RESIDUE PNY A 501
source : AC1

7) chain A
residue 106
type
sequence M
description BINDING SITE FOR RESIDUE PNY A 501
source : AC1

8) chain A
residue 107
type
sequence N
description BINDING SITE FOR RESIDUE PNY A 501
source : AC1

9) chain C
residue 135
type
sequence E
description BINDING SITE FOR RESIDUE PNY A 501
source : AC1

10) chain B
residue 37
type
sequence F
description BINDING SITE FOR RESIDUE PNY B 502
source : AC2

11) chain B
residue 73
type
sequence Q
description BINDING SITE FOR RESIDUE PNY B 502
source : AC2

12) chain B
residue 74
type
sequence L
description BINDING SITE FOR RESIDUE PNY B 502
source : AC2

13) chain B
residue 75
type
sequence T
description BINDING SITE FOR RESIDUE PNY B 502
source : AC2

14) chain B
residue 99
type
sequence Y
description BINDING SITE FOR RESIDUE PNY B 502
source : AC2

15) chain B
residue 103
type
sequence I
description BINDING SITE FOR RESIDUE PNY B 502
source : AC2

16) chain B
residue 106
type
sequence M
description BINDING SITE FOR RESIDUE PNY B 502
source : AC2

17) chain B
residue 107
type
sequence N
description BINDING SITE FOR RESIDUE PNY B 502
source : AC2

18) chain F
residue 135
type
sequence E
description BINDING SITE FOR RESIDUE PNY B 502
source : AC2

19) chain F
residue 139
type
sequence F
description BINDING SITE FOR RESIDUE PNY B 502
source : AC2

20) chain C
residue 73
type
sequence Q
description BINDING SITE FOR RESIDUE PNY C 503
source : AC3

21) chain C
residue 74
type
sequence L
description BINDING SITE FOR RESIDUE PNY C 503
source : AC3

22) chain C
residue 75
type
sequence T
description BINDING SITE FOR RESIDUE PNY C 503
source : AC3

23) chain C
residue 89
type
sequence R
description BINDING SITE FOR RESIDUE PNY C 503
source : AC3

24) chain C
residue 99
type
sequence Y
description BINDING SITE FOR RESIDUE PNY C 503
source : AC3

25) chain C
residue 103
type
sequence I
description BINDING SITE FOR RESIDUE PNY C 503
source : AC3

26) chain C
residue 106
type
sequence M
description BINDING SITE FOR RESIDUE PNY C 503
source : AC3

27) chain C
residue 107
type
sequence N
description BINDING SITE FOR RESIDUE PNY C 503
source : AC3

28) chain E
residue 135
type
sequence E
description BINDING SITE FOR RESIDUE PNY C 503
source : AC3

29) chain B
residue 132
type
sequence L
description BINDING SITE FOR RESIDUE PNY D 504
source : AC4

30) chain B
residue 135
type
sequence E
description BINDING SITE FOR RESIDUE PNY D 504
source : AC4

31) chain D
residue 8
type
sequence P
description BINDING SITE FOR RESIDUE PNY D 504
source : AC4

32) chain D
residue 73
type
sequence Q
description BINDING SITE FOR RESIDUE PNY D 504
source : AC4

33) chain D
residue 74
type
sequence L
description BINDING SITE FOR RESIDUE PNY D 504
source : AC4

34) chain D
residue 75
type
sequence T
description BINDING SITE FOR RESIDUE PNY D 504
source : AC4

35) chain D
residue 99
type
sequence Y
description BINDING SITE FOR RESIDUE PNY D 504
source : AC4

36) chain D
residue 103
type
sequence I
description BINDING SITE FOR RESIDUE PNY D 504
source : AC4

37) chain D
residue 106
type
sequence M
description BINDING SITE FOR RESIDUE PNY D 504
source : AC4

38) chain D
residue 107
type
sequence N
description BINDING SITE FOR RESIDUE PNY D 504
source : AC4

39) chain A
residue 135
type
sequence E
description BINDING SITE FOR RESIDUE PNY E 505
source : AC5

40) chain E
residue 9
type
sequence G
description BINDING SITE FOR RESIDUE PNY E 505
source : AC5

41) chain E
residue 73
type
sequence Q
description BINDING SITE FOR RESIDUE PNY E 505
source : AC5

42) chain E
residue 74
type
sequence L
description BINDING SITE FOR RESIDUE PNY E 505
source : AC5

43) chain E
residue 75
type
sequence T
description BINDING SITE FOR RESIDUE PNY E 505
source : AC5

44) chain E
residue 89
type
sequence R
description BINDING SITE FOR RESIDUE PNY E 505
source : AC5

45) chain E
residue 99
type
sequence Y
description BINDING SITE FOR RESIDUE PNY E 505
source : AC5

46) chain E
residue 106
type
sequence M
description BINDING SITE FOR RESIDUE PNY E 505
source : AC5

47) chain E
residue 107
type
sequence N
description BINDING SITE FOR RESIDUE PNY E 505
source : AC5

48) chain D
residue 135
type
sequence E
description BINDING SITE FOR RESIDUE PNY F 506
source : AC6

49) chain F
residue 74
type
sequence L
description BINDING SITE FOR RESIDUE PNY F 506
source : AC6

50) chain F
residue 75
type
sequence T
description BINDING SITE FOR RESIDUE PNY F 506
source : AC6

51) chain F
residue 99
type
sequence Y
description BINDING SITE FOR RESIDUE PNY F 506
source : AC6

52) chain F
residue 106
type
sequence M
description BINDING SITE FOR RESIDUE PNY F 506
source : AC6

53) chain F
residue 107
type
sequence N
description BINDING SITE FOR RESIDUE PNY F 506
source : AC6

54) chain A
residue 10
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151
source Swiss-Prot : SWS_FT_FI1

55) chain D
residue 10
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151
source Swiss-Prot : SWS_FT_FI1

56) chain D
residue 89
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151
source Swiss-Prot : SWS_FT_FI1

57) chain E
residue 10
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151
source Swiss-Prot : SWS_FT_FI1

58) chain E
residue 89
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151
source Swiss-Prot : SWS_FT_FI1

59) chain F
residue 10
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151
source Swiss-Prot : SWS_FT_FI1

60) chain F
residue 89
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151
source Swiss-Prot : SWS_FT_FI1

61) chain A
residue 89
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151
source Swiss-Prot : SWS_FT_FI1

62) chain B
residue 10
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151
source Swiss-Prot : SWS_FT_FI1

63) chain B
residue 89
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151
source Swiss-Prot : SWS_FT_FI1

64) chain C
residue 10
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151
source Swiss-Prot : SWS_FT_FI1

65) chain C
residue 89
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151
source Swiss-Prot : SWS_FT_FI1

66) chain A
residue 18
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6
source Swiss-Prot : SWS_FT_FI2

67) chain C
residue 90
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6
source Swiss-Prot : SWS_FT_FI2

68) chain C
residue 100
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6
source Swiss-Prot : SWS_FT_FI2

69) chain C
residue 125
type BINDING
sequence Y
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6
source Swiss-Prot : SWS_FT_FI2

70) chain D
residue 18
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6
source Swiss-Prot : SWS_FT_FI2

71) chain D
residue 90
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6
source Swiss-Prot : SWS_FT_FI2

72) chain D
residue 100
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6
source Swiss-Prot : SWS_FT_FI2

73) chain D
residue 125
type BINDING
sequence Y
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6
source Swiss-Prot : SWS_FT_FI2

74) chain E
residue 18
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6
source Swiss-Prot : SWS_FT_FI2

75) chain E
residue 90
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6
source Swiss-Prot : SWS_FT_FI2

76) chain E
residue 100
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6
source Swiss-Prot : SWS_FT_FI2

77) chain A
residue 90
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6
source Swiss-Prot : SWS_FT_FI2

78) chain E
residue 125
type BINDING
sequence Y
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6
source Swiss-Prot : SWS_FT_FI2

79) chain F
residue 18
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6
source Swiss-Prot : SWS_FT_FI2

80) chain F
residue 90
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6
source Swiss-Prot : SWS_FT_FI2

81) chain F
residue 100
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6
source Swiss-Prot : SWS_FT_FI2

82) chain F
residue 125
type BINDING
sequence Y
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6
source Swiss-Prot : SWS_FT_FI2

83) chain A
residue 100
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6
source Swiss-Prot : SWS_FT_FI2

84) chain A
residue 125
type BINDING
sequence Y
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6
source Swiss-Prot : SWS_FT_FI2

85) chain B
residue 18
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6
source Swiss-Prot : SWS_FT_FI2

86) chain B
residue 90
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6
source Swiss-Prot : SWS_FT_FI2

87) chain B
residue 100
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6
source Swiss-Prot : SWS_FT_FI2

88) chain B
residue 125
type BINDING
sequence Y
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6
source Swiss-Prot : SWS_FT_FI2

89) chain C
residue 18
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:21912874, ECO:0007744|PDB:3ND6
source Swiss-Prot : SWS_FT_FI2

90) chain A
residue 75
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000305|PubMed:21912874, ECO:0007744|PDB:3ND7
source Swiss-Prot : SWS_FT_FI3

91) chain B
residue 75
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000305|PubMed:21912874, ECO:0007744|PDB:3ND7
source Swiss-Prot : SWS_FT_FI3

92) chain C
residue 75
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000305|PubMed:21912874, ECO:0007744|PDB:3ND7
source Swiss-Prot : SWS_FT_FI3

93) chain D
residue 75
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000305|PubMed:21912874, ECO:0007744|PDB:3ND7
source Swiss-Prot : SWS_FT_FI3

94) chain E
residue 75
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000305|PubMed:21912874, ECO:0007744|PDB:3ND7
source Swiss-Prot : SWS_FT_FI3

95) chain F
residue 75
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000305|PubMed:21912874, ECO:0007744|PDB:3ND7
source Swiss-Prot : SWS_FT_FI3

96) chain A
residue 18
type SITE
sequence H
description Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00151
source Swiss-Prot : SWS_FT_FI4

97) chain B
residue 18
type SITE
sequence H
description Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00151
source Swiss-Prot : SWS_FT_FI4

98) chain C
residue 18
type SITE
sequence H
description Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00151
source Swiss-Prot : SWS_FT_FI4

99) chain D
residue 18
type SITE
sequence H
description Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00151
source Swiss-Prot : SWS_FT_FI4

100) chain E
residue 18
type SITE
sequence H
description Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00151
source Swiss-Prot : SWS_FT_FI4

101) chain F
residue 18
type SITE
sequence H
description Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00151
source Swiss-Prot : SWS_FT_FI4


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