eF-site ID 1ebd-ABC
PDB Code 1ebd
Chain A, B, C

click to enlarge
Title DIHYDROLIPOAMIDE DEHYDROGENASE COMPLEXED WITH THE BINDING DOMAIN OF THE DIHYDROLIPOAMIDE ACETYLASE
Classification COMPLEX (OXIDOREDUCTASE/TRANSFERASE)
Compound DIHYDROLIPOAMIDE DEHYDROGENASE
Source Geobacillus stearothermophilus (Bacillus stearothermophilus) (ODP2_BACST)
Sequence A:  AIETETLVVGAGPGGYVAAIRAAQLGQKVTIVEKGNLGGV
CLNVGCIPSKALISASHRYEQAKHSEEMGIKAENVTIDFA
KVQEWKASVVKKLTGGVEGLLKGNKVEIVKGEAYFVDANT
VRVVNGDSAQTYTFKNAIIATGSRPIELPNFKFSNRILDS
TGALNLGEVPKSLVVIGGGYIGIELGTAYANFGTKVTILE
GAGEILSGFEKQMAAIIKKRLKKKGVEVVTNALAKGAEER
EDGVTVTYEANGETKTIDADYVLVTVGRRPNTDELGLEQI
GIKMTNRGLIEVDQQCRTSVPNIFAIGDIVPGPALAHKAS
YEGKVAAEAIAGHPSAVDYVAIPAVVFSDPECASVGYFEQ
QAKDEGIDVIAAKFPFAANGRALALNDTDGFLKLVVRKED
GVIIGAQIIGPNASDMIAELGLAIEAGMTAEDIALTIHAH
PTLGEIAMEAAEVAL
B:  AIETETLVVGAGPGGYVAAIRAAQLGQKVTIVEKGNLGGV
CLNVGCIPSKALISASHRYEQAKHSEEMGIKAENVTIDFA
KVQEWKASVVKKLTGGVEGLLKGNKVEIVKGEAYFVDANT
VRVVNGDSAQTYTFKNAIIATGSRPIELPNFKFSNRILDS
TGALNLGEVPKSLVVIGGGYIGIELGTAYANFGTKVTILE
GAGEILSGFEKQMAAIIKKRLKKKGVEVVTNALAKGAEER
EDGVTVTYEANGETKTIDADYVLVTVGRRPNTDELGLEQI
GIKMTNRGLIEVDQQCRTSVPNIFAIGDIVPGPALAHKAS
YEGKVAAEAIAGHPSAVDYVAIPAVVFSDPECASVGYFEQ
QAKDEGIDVIAAKFPFAANGRALALNDTDGFLKLVVRKED
GVIIGAQIIGPNASDMIAELGLAIEAGMTAEDIALTIHAH
PTLGEIAMEAAEVAL
C:  IAMPSVRKYAREKGVDIRLVQGTGKNGRVLKEDIDAFLAG
G
Description (1)  DIHYDROLIPOAMIDE DEHYDROGENASE, DIHYDROLIPOAMIDE ACETYLTRANSFERASE, FLAVIN-ADENINE DINUCLEOTIDE


Functional site

1) chain A
residue 16
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

2) chain A
residue 18
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

3) chain A
residue 19
type
sequence P
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

4) chain A
residue 20
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

5) chain A
residue 38
type
sequence V
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

6) chain A
residue 39
type
sequence E
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

7) chain A
residue 40
type
sequence K
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

8) chain A
residue 45
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

9) chain A
residue 46
type
sequence V
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

10) chain A
residue 47
type
sequence C
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

11) chain A
residue 50
type
sequence V
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

12) chain A
residue 51
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

13) chain A
residue 52
type
sequence C
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

14) chain A
residue 56
type
sequence K
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

15) chain A
residue 117
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

16) chain A
residue 118
type
sequence E
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

17) chain A
residue 119
type
sequence A
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

18) chain A
residue 146
type
sequence A
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

19) chain A
residue 147
type
sequence T
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

20) chain A
residue 148
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

21) chain A
residue 186
type
sequence Y
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

22) chain A
residue 187
type
sequence I
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

23) chain A
residue 274
type
sequence R
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

24) chain A
residue 313
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

25) chain A
residue 314
type
sequence D
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

26) chain A
residue 320
type
sequence A
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

27) chain A
residue 321
type
sequence L
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

28) chain A
residue 322
type
sequence A
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

29) chain B
residue 446
type
sequence H
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

30) chain B
residue 447
type
sequence P
description BINDING SITE FOR RESIDUE FAD A 462
source : AC1

31) chain A
residue 446
type
sequence H
description BINDING SITE FOR RESIDUE FAD B 462
source : AC2

32) chain A
residue 447
type
sequence P
description BINDING SITE FOR RESIDUE FAD B 462
source : AC2

33) chain B
residue 16
type
sequence G
description BINDING SITE FOR RESIDUE FAD B 462
source : AC2

34) chain B
residue 18
type
sequence G
description BINDING SITE FOR RESIDUE FAD B 462
source : AC2

35) chain B
residue 19
type
sequence P
description BINDING SITE FOR RESIDUE FAD B 462
source : AC2

36) chain B
residue 20
type
sequence G
description BINDING SITE FOR RESIDUE FAD B 462
source : AC2

37) chain B
residue 39
type
sequence E
description BINDING SITE FOR RESIDUE FAD B 462
source : AC2

38) chain B
residue 40
type
sequence K
description BINDING SITE FOR RESIDUE FAD B 462
source : AC2

39) chain B
residue 45
type
sequence G
description BINDING SITE FOR RESIDUE FAD B 462
source : AC2

40) chain B
residue 46
type
sequence V
description BINDING SITE FOR RESIDUE FAD B 462
source : AC2

41) chain B
residue 47
type
sequence C
description BINDING SITE FOR RESIDUE FAD B 462
source : AC2

42) chain B
residue 52
type
sequence C
description BINDING SITE FOR RESIDUE FAD B 462
source : AC2

43) chain B
residue 56
type
sequence K
description BINDING SITE FOR RESIDUE FAD B 462
source : AC2

44) chain B
residue 117
type
sequence G
description BINDING SITE FOR RESIDUE FAD B 462
source : AC2

45) chain B
residue 118
type
sequence E
description BINDING SITE FOR RESIDUE FAD B 462
source : AC2

46) chain B
residue 119
type
sequence A
description BINDING SITE FOR RESIDUE FAD B 462
source : AC2

47) chain B
residue 146
type
sequence A
description BINDING SITE FOR RESIDUE FAD B 462
source : AC2

48) chain B
residue 147
type
sequence T
description BINDING SITE FOR RESIDUE FAD B 462
source : AC2

49) chain B
residue 148
type
sequence G
description BINDING SITE FOR RESIDUE FAD B 462
source : AC2

50) chain B
residue 186
type
sequence Y
description BINDING SITE FOR RESIDUE FAD B 462
source : AC2

51) chain B
residue 187
type
sequence I
description BINDING SITE FOR RESIDUE FAD B 462
source : AC2

52) chain B
residue 274
type
sequence R
description BINDING SITE FOR RESIDUE FAD B 462
source : AC2

53) chain B
residue 313
type
sequence G
description BINDING SITE FOR RESIDUE FAD B 462
source : AC2

54) chain B
residue 314
type
sequence D
description BINDING SITE FOR RESIDUE FAD B 462
source : AC2

55) chain B
residue 320
type
sequence A
description BINDING SITE FOR RESIDUE FAD B 462
source : AC2

56) chain B
residue 321
type
sequence L
description BINDING SITE FOR RESIDUE FAD B 462
source : AC2

57) chain B
residue 322
type
sequence A
description BINDING SITE FOR RESIDUE FAD B 462
source : AC2

58) chain A
residue 446
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

59) chain B
residue 446
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

60) chain A
residue 39
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:8805537
source Swiss-Prot : SWS_FT_FI2

61) chain A
residue 56
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:8805537
source Swiss-Prot : SWS_FT_FI2

62) chain A
residue 314
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:8805537
source Swiss-Prot : SWS_FT_FI2

63) chain A
residue 322
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:8805537
source Swiss-Prot : SWS_FT_FI2

64) chain B
residue 39
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:8805537
source Swiss-Prot : SWS_FT_FI2

65) chain B
residue 56
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:8805537
source Swiss-Prot : SWS_FT_FI2

66) chain B
residue 314
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:8805537
source Swiss-Prot : SWS_FT_FI2

67) chain B
residue 322
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:8805537
source Swiss-Prot : SWS_FT_FI2

68) chain A
residue 119
type BINDING
sequence A
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

69) chain A
residue 183
type BINDING
sequence G
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

70) chain A
residue 206
type BINDING
sequence E
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

71) chain A
residue 271
type BINDING
sequence T
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

72) chain B
residue 119
type BINDING
sequence A
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

73) chain B
residue 183
type BINDING
sequence G
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

74) chain B
residue 206
type BINDING
sequence E
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

75) chain B
residue 271
type BINDING
sequence T
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

76) chain A
residue 44-54
type prosite
sequence GGVCLNVGCIP
description PYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGvCLnvGCIP
source prosite : PS00076


Display surface

Download
Links