eF-site ID 1rk2-ABCD
PDB Code 1rk2
Chain A, B, C, D

click to enlarge
Title E. COLI RIBOKINASE COMPLEXED WITH RIBOSE AND ADP, SOLVED IN SPACE GROUP P212121
Classification TRANSFERASE
Compound RIBOKINASE
Source null (RBSK_ECOLI)
Sequence A:  AGSLVVLGSINADHILNLQSFPTPGETVTGNHYQVAFGGK
GANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNID
ITPVSVIKGESTGVALIFVNGEGENVIGIHAGANAALSPA
LVEAQRERIANASALLMQLESPLESVMAAAKIAHQNKTIV
ALNPAPARELPDELLALVDIITPNETEAEKLTGIRVENDE
DAAKAAQVLHEKGIRTVLITLGSRGVWASVNGEGQRVPGF
RVQAVDTIAAGDTFNGALITALLEEKPLPEAIRFAHAAAA
IAVTRKGAQPSVPWREEIDAFLDRQ
B:  QNAGSLVVLGSINADHILNLQSFPTPGETVTGNHYQVAFG
GKGANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDN
IDITPVSVIKGESTGVALIFVNGEGENVIGIHAGANAALS
PALVEAQRERIANASALLMQLESPLESVMAAAKIAHQNKT
IVALNPAPARELPDELLALVDIITPNETEAEKLTGIRVEN
DEDAAKAAQVLHEKGIRTVLITLGSRGVWASVNGEGQRVP
GFRVQAVDTIAAGDTFNGALITALLEEKPLPEAIRFAHAA
AAIAVTRKGAQPSVPWREEIDAFLDRQ
C:  AGSLVVLGSINADHILNLQSFPTPGETVTGNHYQVAFGGK
GANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNID
ITPVSVIKGESTGVALIFVNGEGENVIGIHAGANAALSPA
LVEAQRERIANASALLMQLESPLESVMAAAKIAHQNKTIV
ALNPAPARELPDELLALVDIITPNETEAEKLTGIRVENDE
DAAKAAQVLHEKGIRTVLITLGSRGVWASVNGEGQRVPGF
RVQAVDTIAAGDTFNGALITALLEEKPLPEAIRFAHAAAA
IAVTRKGAQPSVPWREEIDAFLDRQR
D:  AGSLVVLGSINADHILNLQSFPTPGETVTGNHYQVAFGGK
GANQAVAAGRSGANIAFIACTGDDSIGESVRQQLATDNID
ITPVSVIKGESTGVALIFVNGEGENVIGIHAGANAALSPA
LVEAQRERIANASALLMQLESPLESVMAAAKIAHQNKTIV
ALNPAPARELPDELLALVDIITPNETEAEKLTGIRVENDE
DAAKAAQVLHEKGIRTVLITLGSRGVWASVNGEGQRVPGF
RVQAVDTIAAGDTFNGALITALLEEKPLPEAIRFAHAAAA
IAVTRKGAQPSVPWREEIDAFLDRQ
Description


Functional site

1) chain A
residue 255
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI1

2) chain B
residue 255
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI1

3) chain C
residue 255
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI1

4) chain D
residue 255
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI1

5) chain A
residue 14
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

6) chain A
residue 42
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

7) chain A
residue 143
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

8) chain A
residue 187
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

9) chain B
residue 143
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

10) chain B
residue 187
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

11) chain B
residue 223
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

12) chain B
residue 255
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

13) chain B
residue 279
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

14) chain C
residue 14
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

15) chain C
residue 42
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

16) chain C
residue 143
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

17) chain C
residue 187
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

18) chain C
residue 223
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

19) chain C
residue 255
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

20) chain C
residue 279
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

21) chain D
residue 14
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

22) chain D
residue 42
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

23) chain D
residue 143
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

24) chain D
residue 187
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

25) chain D
residue 223
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

26) chain D
residue 255
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

27) chain D
residue 279
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

28) chain A
residue 223
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

29) chain A
residue 255
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

30) chain A
residue 279
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

31) chain B
residue 14
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

32) chain B
residue 42
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
source Swiss-Prot : SWS_FT_FI2

33) chain A
residue 249
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

34) chain A
residue 251
type BINDING
sequence I
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

35) chain A
residue 285
type BINDING
sequence A
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

36) chain A
residue 288
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

37) chain B
residue 288
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

38) chain B
residue 290
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

39) chain B
residue 294
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

40) chain C
residue 249
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

41) chain C
residue 251
type BINDING
sequence I
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

42) chain C
residue 285
type BINDING
sequence A
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

43) chain C
residue 288
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

44) chain C
residue 290
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

45) chain C
residue 294
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

46) chain D
residue 249
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

47) chain D
residue 251
type BINDING
sequence I
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

48) chain D
residue 285
type BINDING
sequence A
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

49) chain D
residue 288
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

50) chain D
residue 290
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

51) chain D
residue 294
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

52) chain A
residue 290
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

53) chain A
residue 294
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

54) chain B
residue 249
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

55) chain B
residue 251
type BINDING
sequence I
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

56) chain B
residue 285
type BINDING
sequence A
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
source Swiss-Prot : SWS_FT_FI3

57) chain A
residue 254
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021
source Swiss-Prot : SWS_FT_FI4

58) chain B
residue 254
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021
source Swiss-Prot : SWS_FT_FI4

59) chain C
residue 254
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021
source Swiss-Prot : SWS_FT_FI4

60) chain D
residue 254
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021
source Swiss-Prot : SWS_FT_FI4

61) chain A
residue 252
type catalytic
sequence A
description 663
source MCSA : MCSA1

62) chain A
residue 253
type catalytic
sequence A
description 663
source MCSA : MCSA1

63) chain A
residue 254
type catalytic
sequence G
description 663
source MCSA : MCSA1

64) chain A
residue 255
type catalytic
sequence D
description 663
source MCSA : MCSA1

65) chain B
residue 252
type catalytic
sequence A
description 663
source MCSA : MCSA2

66) chain B
residue 253
type catalytic
sequence A
description 663
source MCSA : MCSA2

67) chain B
residue 254
type catalytic
sequence G
description 663
source MCSA : MCSA2

68) chain B
residue 255
type catalytic
sequence D
description 663
source MCSA : MCSA2

69) chain C
residue 252
type catalytic
sequence A
description 663
source MCSA : MCSA3

70) chain C
residue 253
type catalytic
sequence A
description 663
source MCSA : MCSA3

71) chain C
residue 254
type catalytic
sequence G
description 663
source MCSA : MCSA3

72) chain C
residue 255
type catalytic
sequence D
description 663
source MCSA : MCSA3

73) chain D
residue 252
type catalytic
sequence A
description 663
source MCSA : MCSA4

74) chain D
residue 253
type catalytic
sequence A
description 663
source MCSA : MCSA4

75) chain D
residue 254
type catalytic
sequence G
description 663
source MCSA : MCSA4

76) chain D
residue 255
type catalytic
sequence D
description 663
source MCSA : MCSA4

77) chain A
residue 249-262
type prosite
sequence DTIAAGDTFNGALI
description PFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. DTiAAGDtfnGALI
source prosite : PS00584


Display surface

Download
Links