eF-site ID 5n6l-AB
PDB Code 5n6l
Chain A, B

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Title Structure of the membrane integral lipoprotein N-acyltransferase Lnt C387A mutant from E. coli
Classification TRANSFERASE
Compound Apolipoprotein N-acyltransferase
Source (LNT_ECOLI)
Sequence A:  FASLIERQRIRLLLALLFGACGTLAFSPYDVWPAAIISLM
GLQALTFNRRPLQSAAIGFCWGFGLFGSGINWVYVSIATF
GGMPGPVNIFLVVLLAAYLSLYTGLFAGVLSRLWPKTTWL
RVAIAAPALWQVTEFLRGWVLTGFPWLQFGYSQIDGPLKG
LAPIMGVEAINFLLMMVSGLLALALVKRNWRPLVVAVVLF
ALPFPLRYIQWFTPQPEKTIQVSMVQGDIPQSLKWDEGQL
LNTLKIYYNATAPLMGKSSLIIWPESAITDLEINQQPFLK
ALDGELRDKGSSLVTGIVDARLNKQNRYDTYNTIITLGKG
APYSYESADRYNKNHLVPFGEFVPLESILRPLAPFFDLPM
SSFSRGPYIQPPLSANGIELTAAIAYEIILGEQVRDNFRP
DTDYLLTISNDAWFGKSIGPWQHFQMARMRALELARPLLR
STNNGITAVIGPQGEIQAMIPQFTREVLTTNVTPTTGLTP
YARTGNWPLWVLTALFGFAAVLMSLR
B:  FASLIERQRIRLLLALLFGACGTLAFSPYDVWPAAIISLM
GLQALTFNRRPLQSAAIGFCWGFGLFGSGINWVYVSIATF
GGMPGPVNIFLVVLLAAYLSLYTGLFAGVLSRLWPKTTWL
RVAIAAPALWQVTEFLRGWVLTGFPWLQFGYSQIDGPLKG
LAPIMGVEAINFLLMMVSGLLALALVKRNWRPLVVAVVLF
ALPFPLRYIQWFTPQPEKTIQVSMVQGDIPQSLKWDEGQL
LNTLKIYYNATAPLMGKSSLIIWPESAITDLEINQQPFLK
ALDGELRDKGSSLVTGIVDARLNKQNRYDTYNTIITLGKG
APYSYESADRYNKNHLVPFGEFVPLESFSRGPYIQPPLSA
NGIELTAAIAYEIILGEQVRDNFRPDTDYLLTISNDAWFG
KSIGPWQHFQMARMRALELARPLLRSTNNGITAVIGPQGE
IQAMIPQFTREVLTTNVTPTTGLTPYARTGNWPLWVLTAL
FGFAAVLMSLR
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 8
type
sequence E
description binding site for residue OLC A 602
source : AC2

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

9) chain A
residue 20
type
sequence F
description binding site for residue OLC A 602
source : AC2

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

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

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

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

14) chain A
residue 121
type
sequence W
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 182
type
sequence L
description binding site for residue OLC A 603
source : AC3

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

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

19) chain A
residue 190
type
sequence R
description binding site for residue OLC A 604
source : AC4

20) chain A
residue 191
type
sequence N
description binding site for residue OLC A 604
source : AC4

21) chain A
residue 195
type
sequence L
description binding site for residue OLC A 604
source : AC4

22) chain A
residue 10
type
sequence Q
description binding site for residue OLC A 605
source : AC5

23) chain A
residue 14
type
sequence L
description binding site for residue OLC A 605
source : AC5

24) chain A
residue 52
type
sequence R
description binding site for residue OLC A 605
source : AC5

25) chain A
residue 55
type
sequence Q
description binding site for residue OLC A 605
source : AC5

26) chain A
residue 61
type
sequence F
description binding site for residue OLC A 605
source : AC5

27) chain A
residue 488
type
sequence N
description binding site for residue OLC A 606
source : AC6

28) chain A
residue 489
type
sequence W
description binding site for residue OLC A 606
source : AC6

29) chain A
residue 492
type
sequence W
description binding site for residue OLC A 606
source : AC6

30) chain A
residue 11
type
sequence R
description binding site for residue OLC A 607
source : AC7

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

32) chain A
residue 65
type
sequence F
description binding site for residue OLC A 607
source : AC7

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

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

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

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

37) chain A
residue 208
type
sequence L
description binding site for residue OLC A 609
source : AC9

38) chain A
residue 213
type
sequence W
description binding site for residue OLC A 609
source : AC9

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

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

41) chain A
residue 361
type
sequence P
description binding site for residue OLC A 610
source : AD1

42) chain A
residue 18
type
sequence L
description binding site for residue OLC A 611
source : AD2

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

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

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

46) chain A
residue 79
type
sequence I
description binding site for residue OLC A 612
source : AD3

47) chain A
residue 97
type
sequence L
description binding site for residue OLC A 612
source : AD3

48) chain A
residue 339
type
sequence V
description binding site for residue OLC A 612
source : AD3

49) chain A
residue 341
type
sequence F
description binding site for residue OLC A 612
source : AD3

50) chain A
residue 416
type
sequence F
description binding site for residue OLC A 612
source : AD3

51) chain A
residue 82
type
sequence F
description binding site for residue OLC A 613
source : AD4

52) chain A
residue 341
type
sequence F
description binding site for residue OLC A 613
source : AD4

53) chain A
residue 415
type
sequence W
description binding site for residue OLC A 613
source : AD4

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

55) chain A
residue 26
type
sequence L
description binding site for residue OLC A 615
source : AD6

56) chain A
residue 30
type
sequence P
description binding site for residue OLC A 615
source : AD6

57) chain A
residue 31
type
sequence Y
description binding site for residue OLC A 615
source : AD6

58) chain A
residue 356
type
sequence P
description binding site for residue OLC A 615
source : AD6

59) chain A
residue 196
type
sequence V
description binding site for residue OLC A 616
source : AD7

60) chain A
residue 200
type
sequence V
description binding site for residue OLC A 616
source : AD7

61) chain A
residue 203
type
sequence A
description binding site for residue OLC A 616
source : AD7

62) chain A
residue 497
type
sequence L
description binding site for residue OLC A 616
source : AD7

63) chain A
residue 197
type
sequence V
description binding site for residue OLC A 617
source : AD8

64) chain A
residue 201
type
sequence L
description binding site for residue OLC A 617
source : AD8

65) chain A
residue 204
type
sequence L
description binding site for residue OLC A 617
source : AD8

66) chain A
residue 146
type
sequence F
description binding site for residue OLC A 618
source : AD9

67) chain A
residue 339
type
sequence V
description binding site for residue OLC A 618
source : AD9

68) chain A
residue 340
type
sequence P
description binding site for residue OLC A 618
source : AD9

69) chain A
residue 54
type
sequence L
description binding site for residue OLC A 619
source : AE1

70) chain B
residue 211
type
sequence I
description binding site for residue OLC A 619
source : AE1

71) chain B
residue 212
type
sequence Q
description binding site for residue OLC A 619
source : AE1

72) chain A
residue 258
type
sequence G
description binding site for residue GOL A 620
source : AE2

73) chain A
residue 259
type
sequence K
description binding site for residue GOL A 620
source : AE2

74) chain A
residue 261
type
sequence S
description binding site for residue GOL A 620
source : AE2

75) chain A
residue 292
type
sequence G
description binding site for residue GOL A 620
source : AE2

76) chain A
residue 141
type
sequence W
description binding site for residue GOL A 621
source : AE3

77) chain A
residue 143
type
sequence L
description binding site for residue GOL A 621
source : AE3

78) chain A
residue 144
type
sequence T
description binding site for residue GOL A 622
source : AE4

79) chain A
residue 346
type
sequence P
description binding site for residue GOL A 622
source : AE4

80) chain A
residue 347
type
sequence L
description binding site for residue GOL A 622
source : AE4

81) chain A
residue 92
type
sequence F
description binding site for residue GOL A 623
source : AE5

82) chain A
residue 9
type
sequence R
description binding site for residue GOL A 624
source : AE6

83) chain A
residue 10
type
sequence Q
description binding site for residue GOL A 624
source : AE6

84) chain A
residue 202
type
sequence F
description binding site for residue GOL A 627
source : AE9

85) chain A
residue 206
type
sequence F
description binding site for residue GOL A 627
source : AE9

86) chain B
residue 22
type
sequence A
description binding site for residue OLC B 601
source : AF1

87) chain B
residue 26
type
sequence L
description binding site for residue OLC B 601
source : AF1

88) chain B
residue 31
type
sequence Y
description binding site for residue OLC B 601
source : AF1

89) chain B
residue 70
type
sequence S
description binding site for residue OLC B 601
source : AF1

90) chain B
residue 73
type
sequence N
description binding site for residue OLC B 601
source : AF1

91) chain A
residue 86
type
sequence P
description binding site for residue OLC B 602
source : AF2

92) chain A
residue 89
type
sequence V
description binding site for residue OLC B 602
source : AF2

93) chain A
residue 92
type
sequence F
description binding site for residue OLC B 602
source : AF2

94) chain B
residue 178
type
sequence M
description binding site for residue OLC B 602
source : AF2

95) chain B
residue 494
type
sequence L
description binding site for residue OLC B 602
source : AF2

96) chain B
residue 498
type
sequence F
description binding site for residue OLC B 602
source : AF2

97) chain B
residue 7
type
sequence I
description binding site for residue OLC B 603
source : AF3

98) chain B
residue 13
type
sequence R
description binding site for residue OLC B 603
source : AF3

99) chain B
residue 46
type
sequence A
description binding site for residue OLC B 603
source : AF3

100) chain B
residue 47
type
sequence L
description binding site for residue OLC B 603
source : AF3

101) chain B
residue 49
type
sequence F
description binding site for residue OLC B 603
source : AF3

102) chain B
residue 134
type
sequence V
description binding site for residue OLC B 604
source : AF4

103) chain B
residue 394
type
sequence E
description binding site for residue OLC B 604
source : AF4

104) chain B
residue 488
type
sequence N
description binding site for residue OLC B 604
source : AF4

105) chain B
residue 489
type
sequence W
description binding site for residue OLC B 604
source : AF4

106) chain B
residue 492
type
sequence W
description binding site for residue OLC B 604
source : AF4

107) chain B
residue 499
type
sequence G
description binding site for residue OLC B 604
source : AF4

108) chain B
residue 54
type
sequence L
description binding site for residue OLC B 605
source : AF5

109) chain B
residue 96
type
sequence L
description binding site for residue OLC B 605
source : AF5

110) chain B
residue 103
type
sequence L
description binding site for residue OLC B 605
source : AF5

111) chain B
residue 210
type
sequence Y
description binding site for residue OLC B 606
source : AF6

112) chain B
residue 211
type
sequence I
description binding site for residue OLC B 606
source : AF6

113) chain B
residue 212
type
sequence Q
description binding site for residue OLC B 606
source : AF6

114) chain B
residue 209
type
sequence R
description binding site for residue OLC B 607
source : AF7

115) chain B
residue 137
type
sequence F
description binding site for residue OLC B 608
source : AF8

116) chain B
residue 141
type
sequence W
description binding site for residue OLC B 608
source : AF8

117) chain B
residue 488
type
sequence N
description binding site for residue OLC B 608
source : AF8

118) chain B
residue 492
type
sequence W
description binding site for residue OLC B 608
source : AF8

119) chain B
residue 141
type
sequence W
description binding site for residue GOL B 609
source : AF9

120) chain B
residue 143
type
sequence L
description binding site for residue GOL B 609
source : AF9

121) chain B
residue 144
type
sequence T
description binding site for residue GOL B 609
source : AF9

122) chain A
residue 239
type
sequence E
description binding site for residue GOL B 610
source : AG1

123) chain A
residue 277
type
sequence Q
description binding site for residue GOL B 610
source : AG1

124) chain B
residue 277
type
sequence Q
description binding site for residue GOL B 610
source : AG1

125) chain B
residue 280
type
sequence F
description binding site for residue GOL B 610
source : AG1

126) chain B
residue 32
type
sequence D
description binding site for residue GOL B 611
source : AG2

127) chain A
residue 247
type
sequence K
description binding site for residue GOL B 612
source : AG3

128) chain A
residue 251
type
sequence N
description binding site for residue GOL B 612
source : AG3

129) chain B
residue 244
type
sequence N
description binding site for residue GOL B 612
source : AG3

130) 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

131) 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

132) 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

133) 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

134) 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

135) 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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

152) 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

153) 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

154) 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

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

156) 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

157) 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

158) 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

159) chain B
residue 211-487
type TOPO_DOM
sequence IQWFTPQPEKTIQVSMVQGDIPQSLKWDEGQLLNTLKIYY
NATAPLMGKSSLIIWPESAITDLEINQQPFLKALDGELRD
KGSSLVTGIVDARLNKQNRYDTYNTIITLGKGAPYSYESA
DRYNKNHLVPFGEFVPLESFSRGPYIQPPLSANGIELTAA
IAYEIILGEQVRDNFRPDTDYLLTISNDAWFGKSIGPWQH
FQMARMRALELARPLLRSTNNGITAVIGPQGEIQAMIPQF
TREVLTTNVTPTTGLTPYARTG
description Periplasmic => ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614
source Swiss-Prot : SWS_FT_FI3

160) 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

161) 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

162) 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

163) 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

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

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


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