eF-site ID 1dku-AB
PDB Code 1dku
Chain A, B

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Title CRYSTAL STRUCTURES OF BACILLUS SUBTILIS PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE: MOLECULAR BASIS OF ALLOSTERIC INHIBITION AND ACTIVATION.
Classification TRANSFERASE
Compound PROTEIN (PHOSPHORIBOSYL PYROPHOSPHATE SYNTHETASE)
Source Bacillus subtilis (strain 168) (KPRS_BACSU)
Sequence A:  NLKIFSLNSNPELAKEIADIVGVQLGKCSVTRFSDGEVQI
NIEESIRGCDCYIIQSTSDPVNEHIMELLIMVDALKRASA
KTINIVIPYYGYARQDRKARSREPITAKLFANLLETAGAT
RVIALDLHAPQIQGFFDIPIDHLMGVPILGEYFEGKNLED
IVIVSPDHGGVTRARKLADRLKAPIAIIDKRMNIVGNIEG
KTAILIDDIIDTAGTITLAANALVENGAKEVYACCTHPVL
SGPAVERINNSTIKELVVTNSIKLKIERFKQLSVGPLLAE
AIIRVHEQQSVSYLF
B:  NLKIFSLNSNPELAKEIADIVGVQLGKCSVTRFSDGEVQI
NIEESIRGCDCYIIQSTSDPVNEHIMELLIMVDALKRASA
KTINIVIPYYGYARQDRKARSREPITAKLFANLLETAGAT
RVIALDLHAPQIQGFFDIPIDHLMGVPILGEYFEGKNLED
IVIVSPDHGGVTRARKLADRLKAPIAIIDKRMNIVGNIEG
KTAILIDDIIDTAGTITLAANALVENGAKEVYACCTHPVL
SGPAVERINNSTIKELVVTNSIKLKIERFKQLSVGPLLAE
AIIRVHEQQSVSYLF
Description


Functional site

1) chain A
residue 105
type
sequence K
description BINDING SITE FOR RESIDUE AP2 B 1001
source : AC1

2) chain A
residue 108
type
sequence S
description BINDING SITE FOR RESIDUE AP2 B 1001
source : AC1

3) chain A
residue 109
type
sequence R
description BINDING SITE FOR RESIDUE AP2 B 1001
source : AC1

4) chain B
residue 52
type
sequence S
description BINDING SITE FOR RESIDUE AP2 B 1001
source : AC1

5) chain B
residue 54
type
sequence R
description BINDING SITE FOR RESIDUE AP2 B 1001
source : AC1

6) chain B
residue 140
type
sequence Q
description BINDING SITE FOR RESIDUE AP2 B 1001
source : AC1

7) chain B
residue 148
type
sequence D
description BINDING SITE FOR RESIDUE AP2 B 1001
source : AC1

8) chain B
residue 149
type
sequence H
description BINDING SITE FOR RESIDUE AP2 B 1001
source : AC1

9) chain B
residue 310
type
sequence S
description BINDING SITE FOR RESIDUE AP2 B 1001
source : AC1

10) chain B
residue 311
type
sequence V
description BINDING SITE FOR RESIDUE AP2 B 1001
source : AC1

11) chain B
residue 312
type
sequence S
description BINDING SITE FOR RESIDUE AP2 B 1001
source : AC1

12) chain B
residue 315
type
sequence F
description BINDING SITE FOR RESIDUE AP2 B 1001
source : AC1

13) chain A
residue 52
type
sequence S
description BINDING SITE FOR RESIDUE AP2 A 1002
source : AC2

14) chain A
residue 54
type
sequence R
description BINDING SITE FOR RESIDUE AP2 A 1002
source : AC2

15) chain A
residue 140
type
sequence Q
description BINDING SITE FOR RESIDUE AP2 A 1002
source : AC2

16) chain A
residue 148
type
sequence D
description BINDING SITE FOR RESIDUE AP2 A 1002
source : AC2

17) chain A
residue 149
type
sequence H
description BINDING SITE FOR RESIDUE AP2 A 1002
source : AC2

18) chain A
residue 310
type
sequence S
description BINDING SITE FOR RESIDUE AP2 A 1002
source : AC2

19) chain A
residue 311
type
sequence V
description BINDING SITE FOR RESIDUE AP2 A 1002
source : AC2

20) chain A
residue 312
type
sequence S
description BINDING SITE FOR RESIDUE AP2 A 1002
source : AC2

21) chain A
residue 315
type
sequence F
description BINDING SITE FOR RESIDUE AP2 A 1002
source : AC2

22) chain B
residue 105
type
sequence K
description BINDING SITE FOR RESIDUE AP2 A 1002
source : AC2

23) chain B
residue 106
type
sequence A
description BINDING SITE FOR RESIDUE AP2 A 1002
source : AC2

24) chain B
residue 107
type
sequence R
description BINDING SITE FOR RESIDUE AP2 A 1002
source : AC2

25) chain B
residue 108
type
sequence S
description BINDING SITE FOR RESIDUE AP2 A 1002
source : AC2

26) chain B
residue 109
type
sequence R
description BINDING SITE FOR RESIDUE AP2 A 1002
source : AC2

27) chain A
residue 101
type
sequence R
description BINDING SITE FOR RESIDUE ABM A 1003
source : AC3

28) chain A
residue 102
type
sequence Q
description BINDING SITE FOR RESIDUE ABM A 1003
source : AC3

29) chain A
residue 106
type
sequence A
description BINDING SITE FOR RESIDUE ABM A 1003
source : AC3

30) chain A
residue 135
type
sequence H
description BINDING SITE FOR RESIDUE ABM A 1003
source : AC3

31) chain B
residue 40
type
sequence F
description BINDING SITE FOR RESIDUE ABM A 1003
source : AC3

32) chain B
residue 42
type
sequence D
description BINDING SITE FOR RESIDUE ABM A 1003
source : AC3

33) chain B
residue 44
type
sequence E
description BINDING SITE FOR RESIDUE ABM A 1003
source : AC3

34) chain A
residue 40
type
sequence F
description BINDING SITE FOR RESIDUE ABM B 1004
source : AC4

35) chain A
residue 42
type
sequence D
description BINDING SITE FOR RESIDUE ABM B 1004
source : AC4

36) chain A
residue 44
type
sequence E
description BINDING SITE FOR RESIDUE ABM B 1004
source : AC4

37) chain B
residue 101
type
sequence R
description BINDING SITE FOR RESIDUE ABM B 1004
source : AC4

38) chain B
residue 102
type
sequence Q
description BINDING SITE FOR RESIDUE ABM B 1004
source : AC4

39) chain B
residue 104
type
sequence R
description BINDING SITE FOR RESIDUE ABM B 1004
source : AC4

40) chain B
residue 106
type
sequence A
description BINDING SITE FOR RESIDUE ABM B 1004
source : AC4

41) chain B
residue 110
type
sequence E
description BINDING SITE FOR RESIDUE ABM B 1004
source : AC4

42) chain B
residue 135
type
sequence H
description BINDING SITE FOR RESIDUE ABM B 1004
source : AC4

43) chain A
residue 197
type ACT_SITE
sequence K
description ACT_SITE => ECO:0000303|PubMed:28031352, ECO:0000305|PubMed:16008562
source Swiss-Prot : SWS_FT_FI1

44) chain B
residue 197
type ACT_SITE
sequence K
description ACT_SITE => ECO:0000303|PubMed:28031352, ECO:0000305|PubMed:16008562
source Swiss-Prot : SWS_FT_FI1

45) chain A
residue 223
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:Q97CA5, ECO:0000255|HAMAP-Rule:MF_00583
source Swiss-Prot : SWS_FT_FI6

46) chain B
residue 223
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:Q97CA5, ECO:0000255|HAMAP-Rule:MF_00583
source Swiss-Prot : SWS_FT_FI6

47) chain A
residue 219-231
type prosite
sequence AILIDDIIDTAGT
description PUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. AILIDDIIDTAgT
source prosite : PS00103

48) chain A
residue 133-148
type prosite
sequence DLHAPQIQGFFDIPID
description PRPP_SYNTHASE Phosphoribosyl pyrophosphate synthase signature. DLHApQIQGFFdiPID
source prosite : PS00114

49) chain A
residue 227
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:10742175, ECO:0000269|PubMed:11790837, ECO:0007744|PDB:1DKR, ECO:0007744|PDB:1IBS
source Swiss-Prot : SWS_FT_FI7

50) chain B
residue 227
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:10742175, ECO:0000269|PubMed:11790837, ECO:0007744|PDB:1DKR, ECO:0007744|PDB:1IBS
source Swiss-Prot : SWS_FT_FI7

51) chain A
residue 42
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000305|PubMed:10742175
source Swiss-Prot : SWS_FT_FI2

52) chain B
residue 42
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000305|PubMed:10742175
source Swiss-Prot : SWS_FT_FI2

53) chain A
residue 101
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:11790837, ECO:0000305|PubMed:10742175, ECO:0007744|PDB:1DKU, ECO:0007744|PDB:1IBS
source Swiss-Prot : SWS_FT_FI3

54) chain B
residue 101
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:11790837, ECO:0000305|PubMed:10742175, ECO:0007744|PDB:1DKU, ECO:0007744|PDB:1IBS
source Swiss-Prot : SWS_FT_FI3

55) chain A
residue 105
type BINDING
sequence K
description BINDING => ECO:0000305|PubMed:10742175, ECO:0007744|PDB:1DKU
source Swiss-Prot : SWS_FT_FI4

56) chain B
residue 310
type BINDING
sequence S
description BINDING => ECO:0000305|PubMed:10742175, ECO:0007744|PDB:1DKU
source Swiss-Prot : SWS_FT_FI4

57) chain A
residue 109
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:10742175, ECO:0007744|PDB:1DKU
source Swiss-Prot : SWS_FT_FI4

58) chain A
residue 140
type BINDING
sequence Q
description BINDING => ECO:0000305|PubMed:10742175, ECO:0007744|PDB:1DKU
source Swiss-Prot : SWS_FT_FI4

59) chain A
residue 148
type BINDING
sequence D
description BINDING => ECO:0000305|PubMed:10742175, ECO:0007744|PDB:1DKU
source Swiss-Prot : SWS_FT_FI4

60) chain A
residue 310
type BINDING
sequence S
description BINDING => ECO:0000305|PubMed:10742175, ECO:0007744|PDB:1DKU
source Swiss-Prot : SWS_FT_FI4

61) chain B
residue 105
type BINDING
sequence K
description BINDING => ECO:0000305|PubMed:10742175, ECO:0007744|PDB:1DKU
source Swiss-Prot : SWS_FT_FI4

62) chain B
residue 109
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:10742175, ECO:0007744|PDB:1DKU
source Swiss-Prot : SWS_FT_FI4

63) chain B
residue 140
type BINDING
sequence Q
description BINDING => ECO:0000305|PubMed:10742175, ECO:0007744|PDB:1DKU
source Swiss-Prot : SWS_FT_FI4

64) chain B
residue 148
type BINDING
sequence D
description BINDING => ECO:0000305|PubMed:10742175, ECO:0007744|PDB:1DKU
source Swiss-Prot : SWS_FT_FI4

65) chain A
residue 135
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:28031352, ECO:0000305|PubMed:11790837, ECO:0007744|PDB:1IBS
source Swiss-Prot : SWS_FT_FI5

66) chain A
residue 174
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:28031352, ECO:0000305|PubMed:11790837, ECO:0007744|PDB:1IBS
source Swiss-Prot : SWS_FT_FI5

67) chain B
residue 135
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:28031352, ECO:0000305|PubMed:11790837, ECO:0007744|PDB:1IBS
source Swiss-Prot : SWS_FT_FI5

68) chain B
residue 174
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:28031352, ECO:0000305|PubMed:11790837, ECO:0007744|PDB:1IBS
source Swiss-Prot : SWS_FT_FI5


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