eF-site ID 3o8l-A
PDB Code 3o8l
Chain A

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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


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