eF-site ID 2cnm-ABC
PDB Code 2cnm
Chain A, B, C

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Title RimI - Ribosomal S18 N-alpha-protein acetyltransferase in complex with a bisubstrate inhibitor (Cterm-Arg-Arg-Phe-Tyr-Arg-Ala-N-alpha- acetyl-S-CoA).
Classification TRANSFERASE
Compound MODIFICATION OF 30S RIBOSOMAL SUBUNIT PROTEIN S18
Source (V2H9S5_SALET)
Sequence A:  MNTISILSTTDLPAAWQIEQRAHAFPWSEKTFFGNQGERY
LNLKLTADDRMAAFAITQVVLDEATLFNIAVDPDFQRRGL
GRMLLEHLIDELETRGVVTLWLEVRASNAAAIALYESLGF
NEATIRRNYYPTAQGHEDAIIMALPISMKLH
B:  MNTISILSTTDLPAAWQIEQRAHAFPWSEKTFFGNQGERY
LNLKLTADDRMAAFAITQVVLDEATLFNIAVDPDFQRRGL
GRMLLEHLIDELETRGVVTLWLEVRASNAAAIALYESLGF
NEATIRRNYYPTAQGHEDAIIMALPISMKLH
C:  MNTISILSTTDLPAAWQIEQRAHAFPWSEKTFFGNQGERY
LNLKLTADDRMAAFAITQVVLDEATLFNIAVDPDFQRRGL
GRMLLEHLIDELETRGVVTLWLEVRASNAAAIALYESLGF
NEATIRRNYYPTAQGHEDAIIMALPISMKLH
Description (1)  MODIFICATION OF 30S RIBOSOMAL SUBUNIT PROTEIN S18 (E.C.2.3.1.128), 30S RIBOSOMAL PROTEIN S18


Functional site

1) chain A
residue 22
type
sequence A
description BINDING SITE FOR RESIDUE COA D 0
source : AC1

2) chain A
residue 23
type
sequence H
description BINDING SITE FOR RESIDUE COA D 0
source : AC1

3) chain A
residue 69
type
sequence I
description BINDING SITE FOR RESIDUE COA D 0
source : AC1

4) chain A
residue 70
type
sequence A
description BINDING SITE FOR RESIDUE COA D 0
source : AC1

5) chain A
residue 71
type
sequence V
description BINDING SITE FOR RESIDUE COA D 0
source : AC1

6) chain A
residue 76
type
sequence Q
description BINDING SITE FOR RESIDUE COA D 0
source : AC1

7) chain A
residue 77
type
sequence R
description BINDING SITE FOR RESIDUE COA D 0
source : AC1

8) chain A
residue 78
type
sequence R
description BINDING SITE FOR RESIDUE COA D 0
source : AC1

9) chain A
residue 79
type
sequence G
description BINDING SITE FOR RESIDUE COA D 0
source : AC1

10) chain A
residue 81
type
sequence G
description BINDING SITE FOR RESIDUE COA D 0
source : AC1

11) chain A
residue 82
type
sequence R
description BINDING SITE FOR RESIDUE COA D 0
source : AC1

12) chain A
residue 103
type
sequence E
description BINDING SITE FOR RESIDUE COA D 0
source : AC1

13) chain A
residue 104
type
sequence V
description BINDING SITE FOR RESIDUE COA D 0
source : AC1

14) chain A
residue 108
type
sequence N
description BINDING SITE FOR RESIDUE COA D 0
source : AC1

15) chain A
residue 110
type
sequence A
description BINDING SITE FOR RESIDUE COA D 0
source : AC1

16) chain A
residue 113
type
sequence A
description BINDING SITE FOR RESIDUE COA D 0
source : AC1

17) chain A
residue 114
type
sequence L
description BINDING SITE FOR RESIDUE COA D 0
source : AC1

18) chain A
residue 115
type
sequence Y
description BINDING SITE FOR RESIDUE COA D 0
source : AC1

19) chain A
residue 133
type
sequence A
description BINDING SITE FOR RESIDUE COA E 0
source : AC2

20) chain A
residue 134
type
sequence Q
description BINDING SITE FOR RESIDUE COA E 0
source : AC2

21) chain B
residue 22
type
sequence A
description BINDING SITE FOR RESIDUE COA E 0
source : AC2

22) chain B
residue 23
type
sequence H
description BINDING SITE FOR RESIDUE COA E 0
source : AC2

23) chain B
residue 69
type
sequence I
description BINDING SITE FOR RESIDUE COA E 0
source : AC2

24) chain B
residue 70
type
sequence A
description BINDING SITE FOR RESIDUE COA E 0
source : AC2

25) chain B
residue 71
type
sequence V
description BINDING SITE FOR RESIDUE COA E 0
source : AC2

26) chain B
residue 76
type
sequence Q
description BINDING SITE FOR RESIDUE COA E 0
source : AC2

27) chain B
residue 77
type
sequence R
description BINDING SITE FOR RESIDUE COA E 0
source : AC2

28) chain B
residue 78
type
sequence R
description BINDING SITE FOR RESIDUE COA E 0
source : AC2

29) chain B
residue 79
type
sequence G
description BINDING SITE FOR RESIDUE COA E 0
source : AC2

30) chain B
residue 80
type
sequence L
description BINDING SITE FOR RESIDUE COA E 0
source : AC2

31) chain B
residue 81
type
sequence G
description BINDING SITE FOR RESIDUE COA E 0
source : AC2

32) chain B
residue 82
type
sequence R
description BINDING SITE FOR RESIDUE COA E 0
source : AC2

33) chain B
residue 103
type
sequence E
description BINDING SITE FOR RESIDUE COA E 0
source : AC2

34) chain B
residue 108
type
sequence N
description BINDING SITE FOR RESIDUE COA E 0
source : AC2

35) chain B
residue 110
type
sequence A
description BINDING SITE FOR RESIDUE COA E 0
source : AC2

36) chain B
residue 113
type
sequence A
description BINDING SITE FOR RESIDUE COA E 0
source : AC2

37) chain B
residue 115
type
sequence Y
description BINDING SITE FOR RESIDUE COA E 0
source : AC2

38) chain C
residue 22
type
sequence A
description BINDING SITE FOR RESIDUE COA F 0
source : AC3

39) chain C
residue 23
type
sequence H
description BINDING SITE FOR RESIDUE COA F 0
source : AC3

40) chain C
residue 69
type
sequence I
description BINDING SITE FOR RESIDUE COA F 0
source : AC3

41) chain C
residue 70
type
sequence A
description BINDING SITE FOR RESIDUE COA F 0
source : AC3

42) chain C
residue 71
type
sequence V
description BINDING SITE FOR RESIDUE COA F 0
source : AC3

43) chain C
residue 76
type
sequence Q
description BINDING SITE FOR RESIDUE COA F 0
source : AC3

44) chain C
residue 77
type
sequence R
description BINDING SITE FOR RESIDUE COA F 0
source : AC3

45) chain C
residue 78
type
sequence R
description BINDING SITE FOR RESIDUE COA F 0
source : AC3

46) chain C
residue 79
type
sequence G
description BINDING SITE FOR RESIDUE COA F 0
source : AC3

47) chain C
residue 80
type
sequence L
description BINDING SITE FOR RESIDUE COA F 0
source : AC3

48) chain C
residue 81
type
sequence G
description BINDING SITE FOR RESIDUE COA F 0
source : AC3

49) chain C
residue 82
type
sequence R
description BINDING SITE FOR RESIDUE COA F 0
source : AC3

50) chain C
residue 90
type
sequence D
description BINDING SITE FOR RESIDUE COA F 0
source : AC3

51) chain C
residue 103
type
sequence E
description BINDING SITE FOR RESIDUE COA F 0
source : AC3

52) chain C
residue 108
type
sequence N
description BINDING SITE FOR RESIDUE COA F 0
source : AC3

53) chain C
residue 110
type
sequence A
description BINDING SITE FOR RESIDUE COA F 0
source : AC3

54) chain C
residue 111
type
sequence A
description BINDING SITE FOR RESIDUE COA F 0
source : AC3

55) chain C
residue 114
type
sequence L
description BINDING SITE FOR RESIDUE COA F 0
source : AC3

56) chain C
residue 115
type
sequence Y
description BINDING SITE FOR RESIDUE COA F 0
source : AC3

57) chain C
residue 149
type
sequence K
description BINDING SITE FOR RESIDUE COA F 0
source : AC3

58) chain A
residue 69
type BINDING
sequence I
description BINDING => ECO:0000255|HAMAP-Rule:MF_02210, ECO:0000269|PubMed:18596200
source Swiss-Prot : SWS_FT_FI3

59) chain A
residue 77
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_02210, ECO:0000269|PubMed:18596200
source Swiss-Prot : SWS_FT_FI3

60) chain A
residue 108
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_02210, ECO:0000269|PubMed:18596200
source Swiss-Prot : SWS_FT_FI3

61) chain B
residue 69
type BINDING
sequence I
description BINDING => ECO:0000255|HAMAP-Rule:MF_02210, ECO:0000269|PubMed:18596200
source Swiss-Prot : SWS_FT_FI3

62) chain B
residue 77
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_02210, ECO:0000269|PubMed:18596200
source Swiss-Prot : SWS_FT_FI3

63) chain B
residue 108
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_02210, ECO:0000269|PubMed:18596200
source Swiss-Prot : SWS_FT_FI3

64) chain C
residue 69
type BINDING
sequence I
description BINDING => ECO:0000255|HAMAP-Rule:MF_02210, ECO:0000269|PubMed:18596200
source Swiss-Prot : SWS_FT_FI3

65) chain C
residue 77
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_02210, ECO:0000269|PubMed:18596200
source Swiss-Prot : SWS_FT_FI3

66) chain C
residue 108
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_02210, ECO:0000269|PubMed:18596200
source Swiss-Prot : SWS_FT_FI3

67) chain A
residue 115
type ACT_SITE
sequence Y
description Proton donor => ECO:0000255|HAMAP-Rule:MF_02210, ECO:0000305|PubMed:18596200
source Swiss-Prot : SWS_FT_FI2

68) chain B
residue 115
type ACT_SITE
sequence Y
description Proton donor => ECO:0000255|HAMAP-Rule:MF_02210, ECO:0000305|PubMed:18596200
source Swiss-Prot : SWS_FT_FI2

69) chain C
residue 115
type ACT_SITE
sequence Y
description Proton donor => ECO:0000255|HAMAP-Rule:MF_02210, ECO:0000305|PubMed:18596200
source Swiss-Prot : SWS_FT_FI2


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