eF-site ID 3o8l-AB
PDB Code 3o8l
Chain A, B

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Title Structure of phosphofructokinase from rabbit skeletal muscle
Classification TRANSFERASE
Compound 6-phosphofructokinase, muscle type
Source Oryctolagus cuniculus (Rabbit) (K6PF_RABIT)
Sequence A:  ARTLGVGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGARV
FFVHEGYQGLVDGGDHIREATWESVSMMLQLGGTVIGSAR
CKDFREREGRLRAAHNLVKRGITNLCVIGGDGSLTGADTF
RSEWSDLLSDLQKAGKITAEEATRSSYLNIVGLVGSIDND
FCGTDMTIGTDSALHRITEIVDAITTTAQSHQRTFVLEVM
GRHCGYLALVTSLSCGADWVFIPECPPDDNWEDHLCRRLS
ETRTRGSRLNIIIVAEGAIDRNGKPITSEGVKDLVVRRLG
YDTRVTVLGHVQRGGTPSAFDRILGSRMGVEAVMALLEGT
PDTPACVVSLSGNQAVRLPLMECVQVTKDVTKAMDEKRFD
EAMKLRGRSFMNNWEVYKLLAHIRPPAPKSGSYTVAVMNV
GAPAAGMNAAVRSTVRIGLIQGNRVLVVHDGFEGPAKGQI
EEAGWSYVGGWTGQGGSKLGSKRTLPKKSFEQISANITKF
NIQGLVIIGGFEAYTGGLELMEGRKQFDELCIPFVVIPAT
VSNNVPGSDFSVGADTALNTICTTCDRIKQSAAGTKRRVF
IIETMGGYCGYLATMAGLAAGADAAYIFEEPFTIRDLQAN
VEHLVQKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEG
KGIFDSRKNVLGHMQQGGSPTPFDRNFATKMGAKAMNWMA
GKIKESYRNGRIFANTPDSGCVLGMRKRALVFQPVTELQN
QTDFEHRIPKEQWWLKLRPILKILAKYE
B:  ARTLGVGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGARV
FFVHEGYQGLVDGGDHIREATWESVSMMLQLGGTVIGSAR
CKDFREREGRLRAAHNLVKRGITNLCVIGGDGSLTGADTF
RSEWSDLLSDLQKAGKITAEEATRSSYLNIVGLVGSIDND
FCGTDMTIGTDSALHRITEIVDAITTTAQSHQRTFVLEVM
GRHCGYLALVTSLSCGADWVFIPECPPDDNWEDHLCRRLS
ETRTRGSRLNIIIVAEGAIDRNGKPITSEGVKDLVVRRLG
YDTRVTVLGHVQRGGTPSAFDRILGSRMGVEAVMALLEGT
PDTPACVVSLSGNQAVRLPLMECVQVTKDVTKAMDEKRFD
EAMKLRGRSFMNNWEVYKLLAHIRPPAPKSGSYTVAVMNV
GAPAAGMNAAVRSTVRIGLIQGNRVLVVHDGFEGPAKGQI
EEAGWSYVGGWTGQGGSKLGSKRTLPKKSFEQISANITKF
NIQGLVIIGGFEAYTGGLELMEGRKQFDELCIPFVVIPAT
VSNNVPGSDFSVGADTALNTICTTCDRIKQSAAGTKRRVF
IIETMGGYCGYLATMAGLAAGADAAYIFEEPFTIRDLQAN
VEHLVQKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEG
KGIFDSRKNVLGHMQQGGSPTPFDRNFATKMGAKAMNWMA
GKIKESYRNGRIFANTPDSGCVLGMRKRALVFQPVTELQN
QTDFEHRIPKEQWWLKLRPILKILAKYE
Description


Functional site

1) chain A
residue 23
type
sequence S
description BINDING SITE FOR RESIDUE ATP A 763
source : AC1

2) chain A
residue 24
type
sequence G
description BINDING SITE FOR RESIDUE ATP A 763
source : AC1

3) chain A
residue 55
type
sequence Y
description BINDING SITE FOR RESIDUE ATP A 763
source : AC1

4) chain A
residue 88
type
sequence R
description BINDING SITE FOR RESIDUE ATP A 763
source : AC1

5) chain A
residue 89
type
sequence C
description BINDING SITE FOR RESIDUE ATP A 763
source : AC1

6) chain A
residue 90
type
sequence K
description BINDING SITE FOR RESIDUE ATP A 763
source : AC1

7) chain A
residue 118
type
sequence G
description BINDING SITE FOR RESIDUE ATP A 763
source : AC1

8) chain A
residue 120
type
sequence G
description BINDING SITE FOR RESIDUE ATP A 763
source : AC1

9) chain A
residue 121
type
sequence S
description BINDING SITE FOR RESIDUE ATP A 763
source : AC1

10) chain A
residue 123
type
sequence T
description BINDING SITE FOR RESIDUE ATP A 763
source : AC1

11) chain A
residue 124
type
sequence G
description BINDING SITE FOR RESIDUE ATP A 763
source : AC1

12) chain A
residue 173
type
sequence D
description BINDING SITE FOR RESIDUE ADP A 764
source : AC2

13) chain A
residue 174
type
sequence M
description BINDING SITE FOR RESIDUE ADP A 764
source : AC2

14) chain A
residue 214
type
sequence Y
description BINDING SITE FOR RESIDUE ADP A 764
source : AC2

15) chain A
residue 308
type
sequence F
description BINDING SITE FOR RESIDUE ADP A 764
source : AC2

16) chain A
residue 341
type
sequence N
description BINDING SITE FOR RESIDUE ADP A 764
source : AC2

17) chain A
residue 377
type
sequence S
description BINDING SITE FOR RESIDUE ADP A 764
source : AC2

18) chain A
residue 381
type
sequence N
description BINDING SITE FOR RESIDUE ADP A 764
source : AC2

19) chain A
residue 538
type
sequence F
description BINDING SITE FOR RESIDUE ADP A 764
source : AC2

20) chain A
residue 543
type
sequence D
description BINDING SITE FOR RESIDUE ADP A 764
source : AC2

21) chain A
residue 671
type
sequence F
description BINDING SITE FOR RESIDUE ADP A 764
source : AC2

22) chain A
residue 227
type
sequence W
description BINDING SITE FOR RESIDUE ATP A 765
source : AC3

23) chain A
residue 228
type
sequence V
description BINDING SITE FOR RESIDUE ATP A 765
source : AC3

24) chain A
residue 242
type
sequence H
description BINDING SITE FOR RESIDUE ATP A 765
source : AC3

25) chain A
residue 246
type
sequence R
description BINDING SITE FOR RESIDUE ATP A 765
source : AC3

26) chain A
residue 385
type
sequence Y
description BINDING SITE FOR RESIDUE ATP A 765
source : AC3

27) chain A
residue 386
type
sequence K
description BINDING SITE FOR RESIDUE ATP A 765
source : AC3

28) chain A
residue 390
type
sequence H
description BINDING SITE FOR RESIDUE ATP A 765
source : AC3

29) chain A
residue 391
type
sequence I
description BINDING SITE FOR RESIDUE ATP A 765
source : AC3

30) chain B
residue 24
type
sequence G
description BINDING SITE FOR RESIDUE ATP B 763
source : AC4

31) chain B
residue 25
type
sequence G
description BINDING SITE FOR RESIDUE ATP B 763
source : AC4

32) chain B
residue 55
type
sequence Y
description BINDING SITE FOR RESIDUE ATP B 763
source : AC4

33) chain B
residue 88
type
sequence R
description BINDING SITE FOR RESIDUE ATP B 763
source : AC4

34) chain B
residue 89
type
sequence C
description BINDING SITE FOR RESIDUE ATP B 763
source : AC4

35) chain B
residue 90
type
sequence K
description BINDING SITE FOR RESIDUE ATP B 763
source : AC4

36) chain B
residue 118
type
sequence G
description BINDING SITE FOR RESIDUE ATP B 763
source : AC4

37) chain B
residue 119
type
sequence D
description BINDING SITE FOR RESIDUE ATP B 763
source : AC4

38) chain B
residue 120
type
sequence G
description BINDING SITE FOR RESIDUE ATP B 763
source : AC4

39) chain B
residue 121
type
sequence S
description BINDING SITE FOR RESIDUE ATP B 763
source : AC4

40) chain B
residue 123
type
sequence T
description BINDING SITE FOR RESIDUE ATP B 763
source : AC4

41) chain B
residue 124
type
sequence G
description BINDING SITE FOR RESIDUE ATP B 763
source : AC4

42) chain B
residue 166
type
sequence D
description BINDING SITE FOR RESIDUE ATP B 763
source : AC4

43) chain B
residue 168
type
sequence D
description BINDING SITE FOR RESIDUE ATP B 763
source : AC4

44) chain B
residue 173
type
sequence D
description BINDING SITE FOR RESIDUE ADP B 764
source : AC5

45) chain B
residue 174
type
sequence M
description BINDING SITE FOR RESIDUE ADP B 764
source : AC5

46) chain B
residue 214
type
sequence Y
description BINDING SITE FOR RESIDUE ADP B 764
source : AC5

47) chain B
residue 308
type
sequence F
description BINDING SITE FOR RESIDUE ADP B 764
source : AC5

48) chain B
residue 341
type
sequence N
description BINDING SITE FOR RESIDUE ADP B 764
source : AC5

49) chain B
residue 377
type
sequence S
description BINDING SITE FOR RESIDUE ADP B 764
source : AC5

50) chain B
residue 381
type
sequence N
description BINDING SITE FOR RESIDUE ADP B 764
source : AC5

51) chain B
residue 538
type
sequence F
description BINDING SITE FOR RESIDUE ADP B 764
source : AC5

52) chain B
residue 671
type
sequence F
description BINDING SITE FOR RESIDUE ADP B 764
source : AC5

53) chain B
residue 678
type
sequence K
description BINDING SITE FOR RESIDUE ADP B 764
source : AC5

54) chain B
residue 713
type
sequence M
description BINDING SITE FOR RESIDUE ADP B 764
source : AC5

55) chain B
residue 226
type
sequence D
description BINDING SITE FOR RESIDUE ATP B 765
source : AC6

56) chain B
residue 228
type
sequence V
description BINDING SITE FOR RESIDUE ATP B 765
source : AC6

57) chain B
residue 242
type
sequence H
description BINDING SITE FOR RESIDUE ATP B 765
source : AC6

58) chain B
residue 246
type
sequence R
description BINDING SITE FOR RESIDUE ATP B 765
source : AC6

59) chain B
residue 385
type
sequence Y
description BINDING SITE FOR RESIDUE ATP B 765
source : AC6

60) chain B
residue 386
type
sequence K
description BINDING SITE FOR RESIDUE ATP B 765
source : AC6

61) chain B
residue 389
type
sequence A
description BINDING SITE FOR RESIDUE ATP B 765
source : AC6

62) chain B
residue 390
type
sequence H
description BINDING SITE FOR RESIDUE ATP B 765
source : AC6

63) chain B
residue 391
type
sequence I
description BINDING SITE FOR RESIDUE ATP B 765
source : AC6

64) chain A
residue 35
type
sequence R
description BINDING SITE FOR RESIDUE PO4 A 766
source : AC7

65) chain A
residue 39
type
sequence R
description BINDING SITE FOR RESIDUE PO4 A 766
source : AC7

66) chain A
residue 420
type
sequence R
description BINDING SITE FOR RESIDUE PO4 A 767
source : AC8

67) chain A
residue 424
type
sequence R
description BINDING SITE FOR RESIDUE PO4 A 767
source : AC8

68) chain A
residue 457
type
sequence G
description BINDING SITE FOR RESIDUE PO4 A 767
source : AC8

69) chain A
residue 458
type
sequence G
description BINDING SITE FOR RESIDUE PO4 A 767
source : AC8

70) chain A
residue 471
type
sequence R
description BINDING SITE FOR RESIDUE PO4 A 768
source : AC9

71) chain A
residue 528
type
sequence T
description BINDING SITE FOR RESIDUE PO4 A 768
source : AC9

72) chain A
residue 530
type
sequence S
description BINDING SITE FOR RESIDUE PO4 A 768
source : AC9

73) chain A
residue 532
type
sequence N
description BINDING SITE FOR RESIDUE PO4 A 768
source : AC9

74) chain A
residue 735
type
sequence R
description BINDING SITE FOR RESIDUE PO4 A 768
source : AC9

75) chain B
residue 39
type
sequence R
description BINDING SITE FOR RESIDUE PO4 B 766
source : BC1

76) chain B
residue 74
type
sequence S
description BINDING SITE FOR RESIDUE PO4 B 766
source : BC1

77) chain B
residue 75
type
sequence M
description BINDING SITE FOR RESIDUE PO4 B 766
source : BC1

78) chain B
residue 589
type
sequence G
description BINDING SITE FOR RESIDUE PO4 B 766
source : BC1

79) chain B
residue 224
type
sequence G
description BINDING SITE FOR RESIDUE PO4 B 767
source : BC2

80) chain B
residue 420
type
sequence R
description BINDING SITE FOR RESIDUE PO4 B 767
source : BC2

81) chain B
residue 424
type
sequence R
description BINDING SITE FOR RESIDUE PO4 B 767
source : BC2

82) chain B
residue 457
type
sequence G
description BINDING SITE FOR RESIDUE PO4 B 767
source : BC2

83) chain B
residue 458
type
sequence G
description BINDING SITE FOR RESIDUE PO4 B 767
source : BC2

84) chain B
residue 460
type
sequence T
description BINDING SITE FOR RESIDUE PO4 B 767
source : BC2

85) chain B
residue 471
type
sequence R
description BINDING SITE FOR RESIDUE PO4 B 768
source : BC3

86) chain B
residue 528
type
sequence T
description BINDING SITE FOR RESIDUE PO4 B 768
source : BC3

87) chain B
residue 530
type
sequence S
description BINDING SITE FOR RESIDUE PO4 B 768
source : BC3

88) chain B
residue 532
type
sequence N
description BINDING SITE FOR RESIDUE PO4 B 768
source : BC3

89) chain B
residue 735
type
sequence R
description BINDING SITE FOR RESIDUE PO4 B 768
source : BC3

90) chain A
residue 164
type BINDING
sequence S
description in other chain => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI3

91) chain A
residue 735
type BINDING
sequence R
description in other chain => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI3

92) chain B
residue 164
type BINDING
sequence S
description in other chain => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI3

93) chain B
residue 208
type BINDING
sequence M
description in other chain => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI3

94) chain B
residue 264
type BINDING
sequence E
description in other chain => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI3

95) chain B
residue 298
type BINDING
sequence H
description in other chain => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI3

96) chain B
residue 471
type BINDING
sequence R
description in other chain => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI3

97) chain B
residue 528
type BINDING
sequence T
description in other chain => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI3

98) chain B
residue 573
type BINDING
sequence M
description in other chain => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI3

99) chain B
residue 629
type BINDING
sequence E
description in other chain => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI3

100) chain B
residue 661
type BINDING
sequence H
description in other chain => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI3

101) chain A
residue 208
type BINDING
sequence M
description in other chain => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI3

102) chain B
residue 735
type BINDING
sequence R
description in other chain => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI3

103) chain A
residue 264
type BINDING
sequence E
description in other chain => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI3

104) chain A
residue 298
type BINDING
sequence H
description in other chain => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI3

105) chain A
residue 471
type BINDING
sequence R
description in other chain => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI3

106) chain A
residue 528
type BINDING
sequence T
description in other chain => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI3

107) chain A
residue 573
type BINDING
sequence M
description in other chain => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI3

108) chain A
residue 629
type BINDING
sequence E
description in other chain => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI3

109) chain A
residue 661
type BINDING
sequence H
description in other chain => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI3

110) chain A
residue 133
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P47858
source Swiss-Prot : SWS_FT_FI5

111) chain B
residue 133
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P47858
source Swiss-Prot : SWS_FT_FI5

112) chain A
residue 166
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI1

113) chain B
residue 166
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI1

114) chain A
residue 25
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI2

115) chain B
residue 88
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI2

116) chain B
residue 118
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI2

117) chain B
residue 119
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI2

118) chain B
residue 201
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI2

119) chain B
residue 292
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI2

120) chain B
residue 566
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI2

121) chain B
residue 655
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI2

122) chain A
residue 88
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI2

123) chain A
residue 118
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI2

124) chain A
residue 119
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI2

125) chain A
residue 201
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI2

126) chain A
residue 292
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI2

127) chain A
residue 566
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI2

128) chain A
residue 655
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI2

129) chain B
residue 25
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_03184
source Swiss-Prot : SWS_FT_FI2

130) chain A
residue 377
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P47857
source Swiss-Prot : SWS_FT_FI6

131) chain B
residue 377
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P47857
source Swiss-Prot : SWS_FT_FI6

132) chain A
residue 557
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P08237
source Swiss-Prot : SWS_FT_FI7

133) chain B
residue 557
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P08237
source Swiss-Prot : SWS_FT_FI7

134) chain A
residue 667
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P08237
source Swiss-Prot : SWS_FT_FI8

135) chain B
residue 667
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P08237
source Swiss-Prot : SWS_FT_FI8

136) chain A
residue 530
type CARBOHYD
sequence S
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

137) chain B
residue 530
type CARBOHYD
sequence S
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

138) chain A
residue 292-310
type prosite
sequence RVTVLGHVQRGGTPSAFDR
description PHOSPHOFRUCTOKINASE Phosphofructokinase signature. RvtvlGHvQRGGtpsafDR
source prosite : PS00433

139) chain A
residue 655-673
type prosite
sequence RKNVLGHMQQGGSPTPFDR
description PHOSPHOFRUCTOKINASE Phosphofructokinase signature. RvtvlGHvQRGGtpsafDR
source prosite : PS00433


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