eF-site ID 5n6h-AB
PDB Code 5n6h
Chain A, B

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Title Structure of the membrane integral lipoprotein N-acyltransferase Lnt from E. coli
Classification MEMBRANE PROTEIN
Compound Apolipoprotein N-acyltransferase
Source (LNT_ECOLI)
Sequence A:  LIERQRIRLLLALLFGACGTLAFSPYDVWPAAIISLMGLQ
ALTFNRRPLQSAAIGFCWGFGLFGSGINWVYVSIATFGGM
PGPVNIFLVVLLAAYLSLYTGLFAGVLSRLWPKTTWLRVA
IAAPALWQVTEFLRGWVLTGFPWLQFGYSQIDGPLKGLAP
IMGVEAINFLLMMVSGLLALALVKRNWRPLVVAVVLFALP
FPLRYIQWFTPQPEKTIQVSMVQGDIPQSLKWDEGQLLNT
LKIYYNATAPLMGKSSLIIWPESAITDLEINQQPFLKALD
GELRDKGSSLVTGIVDARLNKQNRYDTYNTIITLGKGAPY
SYESADRYNKNHLVPFGEFVPLESILRPLAPFFDLPMSSF
SRGPYIQPPLSANGIELTAAICYEIILGEQVRDNFRPDTD
YLLTISNDAWFGKSIGPWQHFQMARMRALELARPLLRSTN
NGITAVIGPQGEIQAMIPQFTREVLTTNVTPTTGLTPYAR
TGNWPLWVLTALFGFAAVLMSLR
B:  AFASLIERQRIRLLLALLFGACGTLAFSPYDVWPAAIISL
MGLQALTFNRRPLQSAAIGFCWGFGLFGSGINWVYVSIAT
FGGMPGPVNIFLVVLLAAYLSLYTGLFAGVLSRLWPKTTW
LRVAIAAPALWQVTEFLRGWVLTGFPWLQFGYSQIDGPLK
GLAPIMGVEAINFLLMMVSGLLALALVKRNWRPLVVAVVL
FALPFPLRYIQWFTPQPEKTIQVSMVQGDIPQSLKWDEGQ
LLNTLKIYYNATAPLMGKSSLIIWPESAITDLEINQQPFL
KALDGELRDKGSSLVTGIVDARLNKQNRYDTYNTIITLGK
GAPYSYESADRYNKNHLVPFGEFVPLESILRPLSFSRGPY
IQPPLSANGIELTAAICYEIILGEQVRDNFRPDTDYLLTI
SNDAWFGKSIGPWQHFQMARMRALELARPLLRSTNNGITA
VIGPQGEIQAMIPQFTREVLTTNVTPTTGLTPYARTGNWP
LWVLTALFGFAAVLMSLR
Description


Functional site

1) chain A
residue 22
type
sequence A
description binding site for residue OLC A 601
source : AC1

2) chain A
residue 25
type
sequence T
description binding site for residue OLC A 601
source : AC1

3) chain A
residue 26
type
sequence L
description binding site for residue OLC A 601
source : AC1

4) chain A
residue 31
type
sequence Y
description binding site for residue OLC A 601
source : AC1

5) chain A
residue 70
type
sequence S
description binding site for residue OLC A 601
source : AC1

6) chain A
residue 73
type
sequence N
description binding site for residue OLC A 601
source : AC1

7) chain A
residue 13
type
sequence R
description binding site for residue OLC A 602
source : AC2

8) chain A
residue 46
type
sequence A
description binding site for residue OLC A 602
source : AC2

9) chain A
residue 47
type
sequence L
description binding site for residue OLC A 602
source : AC2

10) chain A
residue 49
type
sequence F
description binding site for residue OLC A 602
source : AC2

11) chain A
residue 50
type
sequence N
description binding site for residue OLC A 602
source : AC2

12) chain A
residue 188
type
sequence V
description binding site for residue OLC A 602
source : AC2

13) chain A
residue 121
type
sequence W
description binding site for residue OLC A 603
source : AC3

14) chain A
residue 171
type
sequence A
description binding site for residue OLC A 603
source : AC3

15) chain A
residue 178
type
sequence M
description binding site for residue OLC A 603
source : AC3

16) chain A
residue 191
type
sequence N
description binding site for residue OLC A 603
source : AC3

17) chain A
residue 197
type
sequence V
description binding site for residue OLC A 603
source : AC3

18) chain A
residue 10
type
sequence Q
description binding site for residue OLC A 604
source : AC4

19) chain A
residue 52
type
sequence R
description binding site for residue OLC A 604
source : AC4

20) chain A
residue 55
type
sequence Q
description binding site for residue OLC A 604
source : AC4

21) chain A
residue 58
type
sequence A
description binding site for residue OLC A 604
source : AC4

22) chain A
residue 61
type
sequence F
description binding site for residue OLC A 604
source : AC4

23) chain A
residue 131
type
sequence L
description binding site for residue OLC A 605
source : AC5

24) chain A
residue 134
type
sequence V
description binding site for residue OLC A 605
source : AC5

25) chain A
residue 488
type
sequence N
description binding site for residue OLC A 605
source : AC5

26) chain A
residue 489
type
sequence W
description binding site for residue OLC A 605
source : AC5

27) chain A
residue 492
type
sequence W
description binding site for residue OLC A 605
source : AC5

28) chain A
residue 499
type
sequence G
description binding site for residue OLC A 605
source : AC5

29) chain A
residue 52
type
sequence R
description binding site for residue OLC A 606
source : AC6

30) chain A
residue 54
type
sequence L
description binding site for residue OLC A 606
source : AC6

31) chain A
residue 107
type
sequence L
description binding site for residue OLC A 606
source : AC6

32) chain A
residue 114
type
sequence R
description binding site for residue OLC A 606
source : AC6

33) chain B
residue 211
type
sequence I
description binding site for residue OLC A 606
source : AC6

34) chain B
residue 212
type
sequence Q
description binding site for residue OLC A 606
source : AC6

35) chain A
residue 18
type
sequence L
description binding site for residue OLC A 607
source : AC7

36) chain A
residue 62
type
sequence C
description binding site for residue OLC A 607
source : AC7

37) chain A
residue 134
type
sequence V
description binding site for residue OLC A 608
source : AC8

38) chain A
residue 137
type
sequence F
description binding site for residue OLC A 608
source : AC8

39) chain A
residue 170
type
sequence E
description binding site for residue OLC A 608
source : AC8

40) chain A
residue 488
type
sequence N
description binding site for residue OLC A 608
source : AC8

41) chain A
residue 492
type
sequence W
description binding site for residue OLC A 608
source : AC8

42) chain A
residue 485
type
sequence R
description binding site for residue OLC A 609
source : AC9

43) chain A
residue 341
type
sequence F
description binding site for residue OLC A 610
source : AD1

44) chain B
residue 192
type
sequence W
description binding site for residue OLC A 610
source : AD1

45) chain A
residue 22
type
sequence A
description binding site for residue OLC A 611
source : AD2

46) chain A
residue 69
type
sequence G
description binding site for residue OLC A 611
source : AD2

47) chain A
residue 73
type
sequence N
description binding site for residue OLC A 611
source : AD2

48) chain A
residue 76
type
sequence Y
description binding site for residue OLC A 611
source : AD2

49) chain A
residue 94
type
sequence V
description binding site for residue OLC A 611
source : AD2

50) chain A
residue 95
type
sequence V
description binding site for residue OLC A 611
source : AD2

51) chain A
residue 190
type
sequence R
description binding site for residue OLC A 612
source : AD3

52) chain A
residue 192
type
sequence W
description binding site for residue OLC A 612
source : AD3

53) chain A
residue 143
type
sequence L
description binding site for residue GOL A 613
source : AD4

54) chain A
residue 141
type
sequence W
description binding site for residue GOL A 614
source : AD5

55) chain A
residue 203
type
sequence A
description binding site for residue GOL A 615
source : AD6

56) chain A
residue 206
type
sequence F
description binding site for residue GOL A 615
source : AD6

57) chain A
residue 239
type
sequence E
description binding site for residue GOL A 616
source : AD7

58) chain A
residue 243
type
sequence L
description binding site for residue GOL A 616
source : AD7

59) chain A
residue 277
type
sequence Q
description binding site for residue GOL A 616
source : AD7

60) chain A
residue 279
type
sequence P
description binding site for residue GOL A 616
source : AD7

61) chain A
residue 280
type
sequence F
description binding site for residue GOL A 616
source : AD7

62) chain A
residue 10
type
sequence Q
description binding site for residue GOL A 617
source : AD8

63) chain A
residue 11
type
sequence R
description binding site for residue GOL A 617
source : AD8

64) chain A
residue 258
type
sequence G
description binding site for residue GOL A 618
source : AD9

65) chain A
residue 259
type
sequence K
description binding site for residue GOL A 618
source : AD9

66) chain A
residue 261
type
sequence S
description binding site for residue GOL A 618
source : AD9

67) chain A
residue 291
type
sequence K
description binding site for residue GOL A 618
source : AD9

68) chain A
residue 292
type
sequence G
description binding site for residue GOL A 618
source : AD9

69) chain A
residue 293
type
sequence S
description binding site for residue GOL A 618
source : AD9

70) chain B
residue 22
type
sequence A
description binding site for residue OLC B 601
source : AE1

71) chain B
residue 26
type
sequence L
description binding site for residue OLC B 601
source : AE1

72) chain B
residue 31
type
sequence Y
description binding site for residue OLC B 601
source : AE1

73) chain B
residue 70
type
sequence S
description binding site for residue OLC B 601
source : AE1

74) chain A
residue 86
type
sequence P
description binding site for residue OLC B 602
source : AE2

75) chain A
residue 88
type
sequence P
description binding site for residue OLC B 602
source : AE2

76) chain A
residue 89
type
sequence V
description binding site for residue OLC B 602
source : AE2

77) chain B
residue 120
type
sequence T
description binding site for residue OLC B 602
source : AE2

78) chain B
residue 121
type
sequence W
description binding site for residue OLC B 602
source : AE2

79) chain B
residue 122
type
sequence L
description binding site for residue OLC B 602
source : AE2

80) chain B
residue 125
type
sequence A
description binding site for residue OLC B 602
source : AE2

81) chain B
residue 7
type
sequence I
description binding site for residue OLC B 603
source : AE3

82) chain B
residue 13
type
sequence R
description binding site for residue OLC B 603
source : AE3

83) chain B
residue 20
type
sequence F
description binding site for residue OLC B 603
source : AE3

84) chain B
residue 46
type
sequence A
description binding site for residue OLC B 603
source : AE3

85) chain B
residue 47
type
sequence L
description binding site for residue OLC B 603
source : AE3

86) chain B
residue 49
type
sequence F
description binding site for residue OLC B 603
source : AE3

87) chain B
residue 50
type
sequence N
description binding site for residue OLC B 603
source : AE3

88) chain B
residue 394
type
sequence E
description binding site for residue OLC B 604
source : AE4

89) chain B
residue 398
type
sequence D
description binding site for residue OLC B 604
source : AE4

90) chain B
residue 489
type
sequence W
description binding site for residue OLC B 604
source : AE4

91) chain B
residue 492
type
sequence W
description binding site for residue OLC B 604
source : AE4

92) chain B
residue 496
type
sequence A
description binding site for residue OLC B 604
source : AE4

93) chain B
residue 499
type
sequence G
description binding site for residue OLC B 604
source : AE4

94) chain A
residue 54
type
sequence L
description binding site for residue OLC B 605
source : AE5

95) chain B
residue 210
type
sequence Y
description binding site for residue OLC B 605
source : AE5

96) chain B
residue 211
type
sequence I
description binding site for residue OLC B 605
source : AE5

97) chain B
residue 212
type
sequence Q
description binding site for residue OLC B 605
source : AE5

98) chain B
residue 32
type
sequence D
description binding site for residue OLC B 606
source : AE6

99) chain B
residue 33
type
sequence V
description binding site for residue OLC B 606
source : AE6

100) chain B
residue 34
type
sequence W
description binding site for residue OLC B 606
source : AE6

101) chain B
residue 35
type
sequence P
description binding site for residue OLC B 606
source : AE6

102) chain B
residue 137
type
sequence F
description binding site for residue GOL B 607
source : AE7

103) chain B
residue 141
type
sequence W
description binding site for residue GOL B 607
source : AE7

104) chain B
residue 141
type
sequence W
description binding site for residue GOL B 608
source : AE8

105) chain B
residue 143
type
sequence L
description binding site for residue GOL B 608
source : AE8

106) chain B
residue 143
type
sequence L
description binding site for residue GOL B 609
source : AE9

107) chain B
residue 346
type
sequence P
description binding site for residue GOL B 609
source : AE9

108) chain B
residue 120
type
sequence T
description binding site for residue GOL B 610
source : AF1

109) chain B
residue 121
type
sequence W
description binding site for residue GOL B 610
source : AF1

110) chain B
residue 114
type
sequence R
description binding site for residue GOL B 611
source : AF2

111) chain B
residue 354
type
sequence L
description binding site for residue GOL B 611
source : AF2

112) chain B
residue 258
type
sequence G
description binding site for residue GOL B 612
source : AF3

113) chain B
residue 259
type
sequence K
description binding site for residue GOL B 612
source : AF3

114) chain B
residue 292
type
sequence G
description binding site for residue GOL B 612
source : AF3

115) chain B
residue 378
type
sequence N
description binding site for residue GOL B 612
source : AF3

116) chain A
residue 49-52
type TOPO_DOM
sequence FNRR
description Cytoplasmic => ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614
source Swiss-Prot : SWS_FT_FI1

117) chain A
residue 117-120
type TOPO_DOM
sequence PKTT
description Cytoplasmic => ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614
source Swiss-Prot : SWS_FT_FI1

118) chain A
residue 190-191
type TOPO_DOM
sequence RN
description Cytoplasmic => ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614
source Swiss-Prot : SWS_FT_FI1

119) chain B
residue 49-52
type TOPO_DOM
sequence FNRR
description Cytoplasmic => ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614
source Swiss-Prot : SWS_FT_FI1

120) chain B
residue 117-120
type TOPO_DOM
sequence PKTT
description Cytoplasmic => ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614
source Swiss-Prot : SWS_FT_FI1

121) chain B
residue 190-191
type TOPO_DOM
sequence RN
description Cytoplasmic => ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614
source Swiss-Prot : SWS_FT_FI1

122) chain A
residue 10-27
type TRANSMEM
sequence QRIRLLLALLFGACGTLA
description Helical => ECO:0000269|PubMed:28675161
source Swiss-Prot : SWS_FT_FI2

123) chain B
residue 34-48
type TRANSMEM
sequence WPAAIISLMGLQALT
description Helical => ECO:0000269|PubMed:28675161
source Swiss-Prot : SWS_FT_FI2

124) chain B
residue 53-68
type TRANSMEM
sequence PLQSAAIGFCWGFGLF
description Helical => ECO:0000269|PubMed:28675161
source Swiss-Prot : SWS_FT_FI2

125) chain B
residue 87-116
type TRANSMEM
sequence GPVNIFLVVLLAAYLSLYTGLFAGVLSRLW
description Helical => ECO:0000269|PubMed:28675161
source Swiss-Prot : SWS_FT_FI2

126) chain B
residue 121-141
type TRANSMEM
sequence WLRVAIAAPALWQVTEFLRGW
description Helical => ECO:0000269|PubMed:28675161
source Swiss-Prot : SWS_FT_FI2

127) chain B
residue 169-189
type TRANSMEM
sequence VEAINFLLMMVSGLLALALVK
description Helical => ECO:0000269|PubMed:28675161
source Swiss-Prot : SWS_FT_FI2

128) chain B
residue 192-210
type TRANSMEM
sequence WRPLVVAVVLFALPFPLRY
description Helical => ECO:0000269|PubMed:28675161
source Swiss-Prot : SWS_FT_FI2

129) chain B
residue 488-508
type TRANSMEM
sequence NWPLWVLTALFGFAAVLMSLR
description Helical => ECO:0000269|PubMed:28675161
source Swiss-Prot : SWS_FT_FI2

130) chain A
residue 34-48
type TRANSMEM
sequence WPAAIISLMGLQALT
description Helical => ECO:0000269|PubMed:28675161
source Swiss-Prot : SWS_FT_FI2

131) chain A
residue 53-68
type TRANSMEM
sequence PLQSAAIGFCWGFGLF
description Helical => ECO:0000269|PubMed:28675161
source Swiss-Prot : SWS_FT_FI2

132) chain A
residue 87-116
type TRANSMEM
sequence GPVNIFLVVLLAAYLSLYTGLFAGVLSRLW
description Helical => ECO:0000269|PubMed:28675161
source Swiss-Prot : SWS_FT_FI2

133) chain A
residue 121-141
type TRANSMEM
sequence WLRVAIAAPALWQVTEFLRGW
description Helical => ECO:0000269|PubMed:28675161
source Swiss-Prot : SWS_FT_FI2

134) chain A
residue 169-189
type TRANSMEM
sequence VEAINFLLMMVSGLLALALVK
description Helical => ECO:0000269|PubMed:28675161
source Swiss-Prot : SWS_FT_FI2

135) chain A
residue 192-210
type TRANSMEM
sequence WRPLVVAVVLFALPFPLRY
description Helical => ECO:0000269|PubMed:28675161
source Swiss-Prot : SWS_FT_FI2

136) chain A
residue 488-508
type TRANSMEM
sequence NWPLWVLTALFGFAAVLMSLR
description Helical => ECO:0000269|PubMed:28675161
source Swiss-Prot : SWS_FT_FI2

137) chain B
residue 10-27
type TRANSMEM
sequence QRIRLLLALLFGACGTLA
description Helical => ECO:0000269|PubMed:28675161
source Swiss-Prot : SWS_FT_FI2

138) chain A
residue 28-33
type TOPO_DOM
sequence FSPYDV
description Periplasmic => ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614
source Swiss-Prot : SWS_FT_FI3

139) chain A
residue 69-86
type TOPO_DOM
sequence GSGINWVYVSIATFGGMP
description Periplasmic => ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614
source Swiss-Prot : SWS_FT_FI3

140) chain A
residue 142-168
type TOPO_DOM
sequence VLTGFPWLQFGYSQIDGPLKGLAPIMG
description Periplasmic => ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614
source Swiss-Prot : SWS_FT_FI3

141) chain A
residue 211-487
type TOPO_DOM
sequence IQWFTPQPEKTIQVSMVQGDIPQSLKWDEGQLLNTLKIYY
NATAPLMGKSSLIIWPESAITDLEINQQPFLKALDGELRD
KGSSLVTGIVDARLNKQNRYDTYNTIITLGKGAPYSYESA
DRYNKNHLVPFGEFVPLESILRPLAPFFDLPMSSFSRGPY
IQPPLSANGIELTAAICYEIILGEQVRDNFRPDTDYLLTI
SNDAWFGKSIGPWQHFQMARMRALELARPLLRSTNNGITA
VIGPQGEIQAMIPQFTREVLTTNVTPTTGLTPYARTG
description Periplasmic => ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614
source Swiss-Prot : SWS_FT_FI3

142) chain B
residue 28-33
type TOPO_DOM
sequence FSPYDV
description Periplasmic => ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614
source Swiss-Prot : SWS_FT_FI3

143) chain B
residue 69-86
type TOPO_DOM
sequence GSGINWVYVSIATFGGMP
description Periplasmic => ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614
source Swiss-Prot : SWS_FT_FI3

144) chain B
residue 142-168
type TOPO_DOM
sequence VLTGFPWLQFGYSQIDGPLKGLAPIMG
description Periplasmic => ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614
source Swiss-Prot : SWS_FT_FI3

145) chain B
residue 211-487
type TOPO_DOM
sequence IQWFTPQPEKTIQVSMVQGDIPQSLKWDEGQLLNTLKIYY
NATAPLMGKSSLIIWPESAITDLEINQQPFLKALDGELRD
KGSSLVTGIVDARLNKQNRYDTYNTIITLGKGAPYSYESA
DRYNKNHLVPFGEFVPLESILRPLSFSRGPYIQPPLSANG
IELTAAICYEIILGEQVRDNFRPDTDYLLTISNDAWFGKS
IGPWQHFQMARMRALELARPLLRSTNNGITAVIGPQGEIQ
AMIPQFTREVLTTNVTPTTGLTPYARTG
description Periplasmic => ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614
source Swiss-Prot : SWS_FT_FI3

146) chain A
residue 267
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01148, ECO:0000305|PubMed:28675161
source Swiss-Prot : SWS_FT_FI4

147) chain B
residue 267
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01148, ECO:0000305|PubMed:28675161
source Swiss-Prot : SWS_FT_FI4

148) chain A
residue 335
type ACT_SITE
sequence K
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01148, ECO:0000305|PubMed:28675161
source Swiss-Prot : SWS_FT_FI5

149) chain B
residue 335
type ACT_SITE
sequence K
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01148, ECO:0000305|PubMed:28675161
source Swiss-Prot : SWS_FT_FI5

150) chain A
residue 387
type ACT_SITE
sequence C
description Nucleophile => ECO:0000255|HAMAP-Rule:MF_01148, ECO:0000305|PubMed:28675161
source Swiss-Prot : SWS_FT_FI6

151) chain B
residue 387
type ACT_SITE
sequence C
description Nucleophile => ECO:0000255|HAMAP-Rule:MF_01148, ECO:0000305|PubMed:28675161
source Swiss-Prot : SWS_FT_FI6


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