eF-site ID 6mv9-AB
PDB Code 6mv9
Chain A, B

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Title X-ray crystal structure of Bacillus subtilis ribonucleotide reductase NrdE alpha subunit with TTP and ADP
Classification OXIDOREDUCTASE
Compound Ribonucleoside-diphosphate reductase
Source (A0A162Q3J9_BACIU)
Sequence A:  KWIQLNNEIMIQKDGKFQFDKDKEAVHSYFVDYINQNTVF
FHNLKEKLDYLVENQYYEEEFLSLYSFEDIKEVFKTAYAK
KFRFPSFMSAFKFYNDYALKTNDKKKILERYEDRISIVAL
FFANGDTEKAKEYVNLMINQEYQPSTPTFLNAGRKRRGEL
VSCFLLEVNDSLNDISRAIDISMQLSKLGGGVSLNLSKLR
AKGEAIKDVENATKGVVGVMKLLDNAFRYADQMGQRQGSG
AAYLNIFHRDINDFLDTKKISAVKTLSIGVVIPDKFVELA
REDKAAYVFYPHTIYKEYGQHMDEMDMNEMYDKFVDNPRV
KKEKINPRKLLEKLAMLRSESGYPYIMFQDNVNKVHANNH
ISKVKFSNLCSEVLQASQVSSYTDYDEEDEIGLDISCNLG
SLNILNVMEHKSIEKTVKLATDSLTHVSETTDIRNAPAVR
RANKAMKSIGLGAMNLHGYLAQNGIAYESPEARDFANTFF
MMVNFYSIQRSAEIAKEKGETFDQYEGSTYATGEYFDKYV
STDFSPKYEKIANLFEGMHIPTTEDWKKLKAFVAEHGMYH
SYRLCIAPTGSISYVQSSTASVMPIMERIEEKTYYPMPGL
ASNNWFFYKEAYDMDMFKVVDMIATIQQHIDQGISFTLFL
KDTMTTRDLNRIDLYAHHRGIKTIYYASCLSCVV
B:  PKWIQLNNEIMIQKDGKFQFDKDKEAVHSYFVDYINQNTV
FFHNLKEKLDYLVENQYYEEEFLSLYSFEDIKEVFKTAYA
KKFRFPSFMSAFKFYNDYALKTNDKKKILERYEDRISIVA
LFFANGDTEKAKEYVNLMINQEYQPSTPTFLNAGRKRRGE
LVSCFLLEVNDSLNDISRAIDISMQLSKLGGGVSLNLSKL
RAKGEAIKDVENATKGVVGVMKLLDNAFRYASGAAYLNIF
HRDINDFLDTKKISADEDVRVKTLSIGVVIPDKFVELARE
DKAAYVFYPHTIYKEYGQHMDEMDMNEMYDKFVDNPRVKK
EKINPRKLLEKLAMLRSESGYPYIMFQDNVNKVHANNHIS
KVKFSNLCSEVLQASQVSSYTDYDEEDEIGLDISCNLGSL
NILNVMEHKSIEKTVKLATDSLTHVSETTDIRNAPAVRRA
NKAMKSIGLGAMNLHGYLAQNGIAYESPEARDFANTFFMM
VNFYSIQRSAEIAKEKGETFDQYEGSTYATGEYFDKYVST
DFSPKYEKIANLFEGMHIPTTEDWKKLKAFVAEHGMYHSY
RLCIAPTGSISYVQSSTASVMPIMERIEERTYGNSKTYYP
MPGLASNNWFFYKEAYDMDMFKVVDMIATIQQHIDQGISF
TLFLKDTMTTRDLNRIDLYAHHRGIKTIYYASCLSCVV
Description


Functional site

1) chain A
residue 177
type
sequence D
description binding site for residue TTP A 801
source : AC1

2) chain A
residue 178
type
sequence S
description binding site for residue TTP A 801
source : AC1

3) chain A
residue 179
type
sequence L
description binding site for residue TTP A 801
source : AC1

4) chain A
residue 182
type
sequence I
description binding site for residue TTP A 801
source : AC1

5) chain A
residue 207
type
sequence R
description binding site for residue TTP A 801
source : AC1

6) chain A
residue 213
type
sequence I
description binding site for residue TTP A 801
source : AC1

7) chain A
residue 214
type
sequence K
description binding site for residue TTP A 801
source : AC1

8) chain A
residue 220
type
sequence T
description binding site for residue TTP A 801
source : AC1

9) chain A
residue 221
type
sequence K
description binding site for residue TTP A 801
source : AC1

10) chain B
residue 194
type
sequence K
description binding site for residue TTP A 801
source : AC1

11) chain B
residue 236
type
sequence Y
description binding site for residue TTP A 801
source : AC1

12) chain B
residue 237
type
sequence A
description binding site for residue TTP A 801
source : AC1

13) chain A
residue 33
type
sequence V
description binding site for residue ADP A 802
source : AC2

14) chain A
residue 34
type
sequence H
description binding site for residue ADP A 802
source : AC2

15) chain A
residue 37
type
sequence F
description binding site for residue ADP A 802
source : AC2

16) chain A
residue 42
type
sequence N
description binding site for residue ADP A 802
source : AC2

17) chain A
residue 89
type
sequence F
description binding site for residue ADP A 802
source : AC2

18) chain A
residue 90
type
sequence R
description binding site for residue ADP A 802
source : AC2

19) chain A
residue 91
type
sequence F
description binding site for residue ADP A 802
source : AC2

20) chain A
residue 194
type
sequence K
description binding site for residue TTP B 801
source : AC4

21) chain A
residue 236
type
sequence Y
description binding site for residue TTP B 801
source : AC4

22) chain A
residue 237
type
sequence A
description binding site for residue TTP B 801
source : AC4

23) chain B
residue 177
type
sequence D
description binding site for residue TTP B 801
source : AC4

24) chain B
residue 178
type
sequence S
description binding site for residue TTP B 801
source : AC4

25) chain B
residue 179
type
sequence L
description binding site for residue TTP B 801
source : AC4

26) chain B
residue 182
type
sequence I
description binding site for residue TTP B 801
source : AC4

27) chain B
residue 207
type
sequence R
description binding site for residue TTP B 801
source : AC4

28) chain B
residue 213
type
sequence I
description binding site for residue TTP B 801
source : AC4

29) chain B
residue 214
type
sequence K
description binding site for residue TTP B 801
source : AC4

30) chain B
residue 220
type
sequence T
description binding site for residue TTP B 801
source : AC4

31) chain B
residue 221
type
sequence K
description binding site for residue TTP B 801
source : AC4

32) chain B
residue 34
type
sequence H
description binding site for residue ADP B 802
source : AC5

33) chain B
residue 37
type
sequence F
description binding site for residue ADP B 802
source : AC5

34) chain B
residue 42
type
sequence N
description binding site for residue ADP B 802
source : AC5

35) chain B
residue 90
type
sequence R
description binding site for residue ADP B 802
source : AC5

36) chain B
residue 91
type
sequence F
description binding site for residue ADP B 802
source : AC5

37) chain A
residue 558-580
type prosite
sequence WKKLKAFVAEHGMYHSYRLCIAP
description RIBORED_LARGE Ribonucleotide reductase large subunit signature. WkkLkafvaehGMYHsyrLCiaP
source prosite : PS00089

38) chain A
residue 380
type ACT_SITE
sequence N
description Proton acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

39) chain A
residue 384
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

40) chain B
residue 380
type ACT_SITE
sequence N
description Proton acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

41) chain B
residue 384
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

42) chain A
residue 382
type ACT_SITE
sequence C
description Cysteine radical intermediate => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

43) chain B
residue 382
type ACT_SITE
sequence C
description Cysteine radical intermediate => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

44) chain A
residue 153
type BINDING
sequence T
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

45) chain B
residue 580
type BINDING
sequence P
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

46) chain A
residue 169
type BINDING
sequence S
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

47) chain A
residue 198
type BINDING
sequence G
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

48) chain A
residue 380
type BINDING
sequence N
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

49) chain A
residue 580
type BINDING
sequence P
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

50) chain B
residue 153
type BINDING
sequence T
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

51) chain B
residue 169
type BINDING
sequence S
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

52) chain B
residue 198
type BINDING
sequence G
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

53) chain B
residue 380
type BINDING
sequence N
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

54) chain A
residue 170
type SITE
sequence C
description Important for hydrogen atom transfer => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

55) chain A
residue 409
type SITE
sequence C
description Important for hydrogen atom transfer => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

56) chain B
residue 170
type SITE
sequence C
description Important for hydrogen atom transfer => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

57) chain B
residue 409
type SITE
sequence C
description Important for hydrogen atom transfer => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

58) chain A
residue 177
type SITE
sequence D
description Allosteric effector binding => ECO:0000250
source Swiss-Prot : SWS_FT_FI5

59) chain A
residue 207
type SITE
sequence R
description Allosteric effector binding => ECO:0000250
source Swiss-Prot : SWS_FT_FI5

60) chain B
residue 177
type SITE
sequence D
description Allosteric effector binding => ECO:0000250
source Swiss-Prot : SWS_FT_FI5

61) chain B
residue 207
type SITE
sequence R
description Allosteric effector binding => ECO:0000250
source Swiss-Prot : SWS_FT_FI5

62) chain A
residue 683
type SITE
sequence Y
description Important for electron transfer => ECO:0000250
source Swiss-Prot : SWS_FT_FI6

63) chain A
residue 684
type SITE
sequence Y
description Important for electron transfer => ECO:0000250
source Swiss-Prot : SWS_FT_FI6

64) chain B
residue 683
type SITE
sequence Y
description Important for electron transfer => ECO:0000250
source Swiss-Prot : SWS_FT_FI6

65) chain B
residue 684
type SITE
sequence Y
description Important for electron transfer => ECO:0000250
source Swiss-Prot : SWS_FT_FI6

66) chain A
residue 695
type SITE
sequence C
description Interacts with thioredoxin/glutaredoxin => ECO:0000250
source Swiss-Prot : SWS_FT_FI7

67) chain A
residue 698
type SITE
sequence C
description Interacts with thioredoxin/glutaredoxin => ECO:0000250
source Swiss-Prot : SWS_FT_FI7

68) chain B
residue 695
type SITE
sequence C
description Interacts with thioredoxin/glutaredoxin => ECO:0000250
source Swiss-Prot : SWS_FT_FI7

69) chain B
residue 698
type SITE
sequence C
description Interacts with thioredoxin/glutaredoxin => ECO:0000250
source Swiss-Prot : SWS_FT_FI7


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