eF-site ID 6no0-AB
PDB Code 6no0
Chain A, B

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Title ADP bound to ATP-grasp fold of Blastocystis hominis succinyl-CoA synthetase
Classification LIGASE
Compound Succinate--CoA ligase [ADP-forming] subunit beta
Source (SUCB_BLAHN)
Sequence A:  MNIHEWQSKQLIQKYGGRAQSGEVAFSPERSRDIAKKLWN
QFPGCKFVVKAQVLAGGRGKGHWEHGMQGGVKLAKTPEEV
YEIANEMIGHKLITKQTGAKGINCNKVMVCGAVKILKEFY
LSILLDRAMGCPVIIATSQGGGIEEVAQKCPECLFKVPIS
VKNGPTNEQLVKLAKDLGLEGDLVQDCVDNVKALYQVFDK
CDSTMVEINPLGVIETPTDEKVICCLDAKIAF
B:  MNIHEWQSKQLIQKYGGRAQSGEVAFSPERSRDIAKKLWN
QFPGCKFVVKAQVLAGGRGKGHWEHGMQGGVKLAKTPEEV
YEIANEMIGHKLITKQTGAKGINCNKVMVCGAVKILKEFY
LSILLDRAMGCPVIIATSQGGEEVAQKCPECLFKVPISVK
NGPTNEQLVKLAKDLGLEGDLVQDCVDNVKALYQVFDKCD
STMVEINPLGVIETPTDEKVICCLDAKIAFD
Description (1)  Succinate--CoA ligase [ADP-forming] subunit beta (E.C.6.2.1.5)


Functional site

1) chain A
residue 20
type
sequence Q
description binding site for residue ADP A 301
source : AC1

2) chain A
residue 48
type
sequence V
description binding site for residue ADP A 301
source : AC1

3) chain A
residue 50
type
sequence K
description binding site for residue ADP A 301
source : AC1

4) chain A
residue 58
type
sequence R
description binding site for residue ADP A 301
source : AC1

5) chain A
residue 59
type
sequence G
description binding site for residue ADP A 301
source : AC1

6) chain A
residue 111
type
sequence G
description binding site for residue ADP A 301
source : AC1

7) chain A
residue 113
type
sequence V
description binding site for residue ADP A 301
source : AC1

8) chain A
residue 115
type
sequence I
description binding site for residue ADP A 301
source : AC1

9) chain A
residue 118
type
sequence E
description binding site for residue ADP A 301
source : AC1

10) chain A
residue 210
type
sequence N
description binding site for residue ADP A 301
source : AC1

11) chain A
residue 211
type
sequence P
description binding site for residue ADP A 301
source : AC1

12) chain A
residue 227
type
sequence L
description binding site for residue ADP A 301
source : AC1

13) chain A
residue 228
type
sequence D
description binding site for residue ADP A 301
source : AC1

14) chain A
residue 210
type
sequence N
description binding site for residue MG A 302
source : AC2

15) chain A
residue 228
type
sequence D
description binding site for residue MG A 302
source : AC2

16) chain A
residue 216
type
sequence E
description binding site for residue MG A 303
source : AC3

17) chain A
residue 220
type
sequence D
description binding site for residue MG A 303
source : AC3

18) chain B
residue 220
type
sequence D
description binding site for residue MG A 303
source : AC3

19) chain B
residue 20
type
sequence Q
description binding site for residue ADP B 301
source : AC4

20) chain B
residue 48
type
sequence V
description binding site for residue ADP B 301
source : AC4

21) chain B
residue 50
type
sequence K
description binding site for residue ADP B 301
source : AC4

22) chain B
residue 57
type
sequence G
description binding site for residue ADP B 301
source : AC4

23) chain B
residue 58
type
sequence R
description binding site for residue ADP B 301
source : AC4

24) chain B
residue 59
type
sequence G
description binding site for residue ADP B 301
source : AC4

25) chain B
residue 111
type
sequence G
description binding site for residue ADP B 301
source : AC4

26) chain B
residue 112
type
sequence A
description binding site for residue ADP B 301
source : AC4

27) chain B
residue 113
type
sequence V
description binding site for residue ADP B 301
source : AC4

28) chain B
residue 115
type
sequence I
description binding site for residue ADP B 301
source : AC4

29) chain B
residue 118
type
sequence E
description binding site for residue ADP B 301
source : AC4

30) chain B
residue 210
type
sequence N
description binding site for residue ADP B 301
source : AC4

31) chain B
residue 211
type
sequence P
description binding site for residue ADP B 301
source : AC4

32) chain B
residue 228
type
sequence D
description binding site for residue ADP B 301
source : AC4

33) chain B
residue 210
type
sequence N
description binding site for residue MG B 302
source : AC5

34) chain B
residue 228
type
sequence D
description binding site for residue MG B 302
source : AC5

35) chain A
residue 50
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_03219
source Swiss-Prot : SWS_FT_FI1

36) chain B
residue 228
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_03219
source Swiss-Prot : SWS_FT_FI1

37) chain A
residue 57
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_03219
source Swiss-Prot : SWS_FT_FI1

38) chain A
residue 118
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_03219
source Swiss-Prot : SWS_FT_FI1

39) chain A
residue 210
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_03219
source Swiss-Prot : SWS_FT_FI1

40) chain A
residue 228
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_03219
source Swiss-Prot : SWS_FT_FI1

41) chain B
residue 50
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_03219
source Swiss-Prot : SWS_FT_FI1

42) chain B
residue 57
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_03219
source Swiss-Prot : SWS_FT_FI1

43) chain B
residue 118
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_03219
source Swiss-Prot : SWS_FT_FI1

44) chain B
residue 210
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_03219
source Swiss-Prot : SWS_FT_FI1

45) chain A
residue 46
type SITE
sequence K
description Important for substrate specificity => ECO:0000305|PubMed:18452512
source Swiss-Prot : SWS_FT_FI2

46) chain A
residue 114
type SITE
sequence K
description Important for substrate specificity => ECO:0000305|PubMed:18452512
source Swiss-Prot : SWS_FT_FI2

47) chain B
residue 46
type SITE
sequence K
description Important for substrate specificity => ECO:0000305|PubMed:18452512
source Swiss-Prot : SWS_FT_FI2

48) chain B
residue 114
type SITE
sequence K
description Important for substrate specificity => ECO:0000305|PubMed:18452512
source Swiss-Prot : SWS_FT_FI2


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