eF-site ID 2bfd-AB
PDB Code 2bfd
Chain A, B

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Title Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch
Classification OXIDOREDUCTASE
Compound 2-OXOISOVALERATE DEHYDROGENASE ALPHA SUBUNIT
Source (ODBB_HUMAN)
Sequence A:  KPQFPGASAEFIDKLEFIQPNVISGIPIYRVMDRQGQIIN
PSEDPHLPKEKVLKLYKSMTLLNTMDRILYESQRQGRISF
YMTNYGEEGTHVGSAAALDNTDLVFGQAREAGVLMYRDYP
LELFMAQCYGNISDLGKGRQMPVHYGCKERHFVTISSPLA
TQIPQAVGAAYAAKRANANRVVICYFGEGAASEGDAHAGF
NFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPG
YGIMSIRVDGNDVFAVYNATKEARRRAVAENQPFLIEAMT
YRIGSTDHPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVM
EAFEQAERKPKPNPNLLFSDVYQEMPAQLRKQQESLARHL
QTYGEHYPLDHFDK
B:  AHFEYGQTQKMNLFQSVTSALDNSLAKDPTAVIFGEDVAF
GGVFRCTVGLRDKYGKDRVFNTPLCEQGIVGFGIGIAVTG
ATAIAEIQFADYIFPAFDQIVNEAAKYRYRSGDLFNCGSL
TIRSPWGCVGHGALYHSQSPEAFFAHCPGIKVVIPRSPFQ
AKGLLLSCIEDKNPCIFFEPKILYRAAAEEVPIEPYNIPL
SQAEVIQEGSDVTLVAWGTQVHVIREVASMAKEKLGVSCE
VIDLRTIIPWDVDTICKSVIKTGRLLISHEAPLTGGFASE
ISSTVQEECFLNLEAPISRVCGYDTPFPHIFEPFYIPDKW
KCYDALRKMINY
Description


Functional site

1) chain A
residue 112
type
sequence Q
description BINDING SITE FOR RESIDUE K A 501
source : AC1

2) chain A
residue 161
type
sequence S
description BINDING SITE FOR RESIDUE K A 501
source : AC1

3) chain A
residue 163
type
sequence P
description BINDING SITE FOR RESIDUE K A 501
source : AC1

4) chain A
residue 166
type
sequence T
description BINDING SITE FOR RESIDUE K A 501
source : AC1

5) chain A
residue 167
type
sequence Q
description BINDING SITE FOR RESIDUE K A 501
source : AC1

6) chain A
residue 193
type
sequence E
description BINDING SITE FOR RESIDUE MN A 503
source : AC2

7) chain A
residue 222
type
sequence N
description BINDING SITE FOR RESIDUE MN A 503
source : AC2

8) chain A
residue 224
type
sequence Y
description BINDING SITE FOR RESIDUE MN A 503
source : AC2

9) chain A
residue 53
type
sequence P
description BINDING SITE FOR RESIDUE CL A 504
source : AC3

10) chain A
residue 55
type
sequence E
description BINDING SITE FOR RESIDUE CL A 504
source : AC3

11) chain A
residue 369
type
sequence Q
description BINDING SITE FOR RESIDUE CL A 504
source : AC3

12) chain B
residue 128
type
sequence G
description BINDING SITE FOR RESIDUE K B 502
source : AC4

13) chain B
residue 130
type
sequence L
description BINDING SITE FOR RESIDUE K B 502
source : AC4

14) chain B
residue 131
type
sequence T
description BINDING SITE FOR RESIDUE K B 502
source : AC4

15) chain B
residue 178
type
sequence C
description BINDING SITE FOR RESIDUE K B 502
source : AC4

16) chain B
residue 181
type
sequence D
description BINDING SITE FOR RESIDUE K B 502
source : AC4

17) chain B
residue 183
type
sequence N
description BINDING SITE FOR RESIDUE K B 502
source : AC4

18) chain A
residue 112
type
sequence Q
description BINDING SITE FOR RESIDUE TPP A 601
source : AC5

19) chain A
residue 114
type
sequence R
description BINDING SITE FOR RESIDUE TPP A 601
source : AC5

20) chain A
residue 162
type
sequence S
description BINDING SITE FOR RESIDUE TPP A 601
source : AC5

21) chain A
residue 164
type
sequence L
description BINDING SITE FOR RESIDUE TPP A 601
source : AC5

22) chain A
residue 192
type
sequence G
description BINDING SITE FOR RESIDUE TPP A 601
source : AC5

23) chain A
residue 193
type
sequence E
description BINDING SITE FOR RESIDUE TPP A 601
source : AC5

24) chain A
residue 194
type
sequence G
description BINDING SITE FOR RESIDUE TPP A 601
source : AC5

25) chain A
residue 195
type
sequence A
description BINDING SITE FOR RESIDUE TPP A 601
source : AC5

26) chain A
residue 198
type
sequence E
description BINDING SITE FOR RESIDUE TPP A 601
source : AC5

27) chain A
residue 220
type
sequence R
description BINDING SITE FOR RESIDUE TPP A 601
source : AC5

28) chain A
residue 222
type
sequence N
description BINDING SITE FOR RESIDUE TPP A 601
source : AC5

29) chain A
residue 224
type
sequence Y
description BINDING SITE FOR RESIDUE TPP A 601
source : AC5

30) chain A
residue 225
type
sequence A
description BINDING SITE FOR RESIDUE TPP A 601
source : AC5

31) chain A
residue 226
type
sequence I
description BINDING SITE FOR RESIDUE TPP A 601
source : AC5

32) chain B
residue 46
type
sequence E
description BINDING SITE FOR RESIDUE TPP A 601
source : AC5

33) chain B
residue 74
type
sequence L
description BINDING SITE FOR RESIDUE TPP A 601
source : AC5

34) chain B
residue 76
type
sequence E
description BINDING SITE FOR RESIDUE TPP A 601
source : AC5

35) chain B
residue 98
type
sequence Q
description BINDING SITE FOR RESIDUE TPP A 601
source : AC5

36) chain B
residue 102
type
sequence Y
description BINDING SITE FOR RESIDUE TPP A 601
source : AC5

37) chain A
residue 374
type
sequence Q
description BINDING SITE FOR RESIDUE GOL B 701
source : AC6

38) chain B
residue 260
type
sequence W
description BINDING SITE FOR RESIDUE GOL B 701
source : AC6

39) chain B
residue 284
type
sequence T
description BINDING SITE FOR RESIDUE GOL B 701
source : AC6

40) chain B
residue 290
type
sequence E
description BINDING SITE FOR RESIDUE GOL B 701
source : AC6

41) chain B
residue 294
type
sequence T
description BINDING SITE FOR RESIDUE GOL B 701
source : AC6

42) chain B
residue 309
type
sequence R
description BINDING SITE FOR RESIDUE GOL B 701
source : AC6

43) chain A
residue 73
type
sequence I
description BINDING SITE FOR RESIDUE MPD B 901
source : AC7

44) chain A
residue 76
type
sequence E
description BINDING SITE FOR RESIDUE MPD B 901
source : AC7

45) chain A
residue 82
type
sequence R
description BINDING SITE FOR RESIDUE MPD B 901
source : AC7

46) chain A
residue 349
type
sequence F
description BINDING SITE FOR RESIDUE MPD B 901
source : AC7

47) chain B
residue 58
type
sequence V
description BINDING SITE FOR RESIDUE MPD B 901
source : AC7

48) chain A
residue 335
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P50136
source Swiss-Prot : SWS_FT_FI6

49) chain A
residue 76
type catalytic
sequence E
description 280
source MCSA : MCSA1

50) chain A
residue 162
type catalytic
sequence S
description 280
source MCSA : MCSA1

51) chain A
residue 292
type catalytic
sequence S
description 280
source MCSA : MCSA1

52) chain B
residue 131
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:10745006, ECO:0007744|PDB:1DTW
source Swiss-Prot : SWS_FT_FI1

53) chain B
residue 178
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:10745006, ECO:0007744|PDB:1DTW
source Swiss-Prot : SWS_FT_FI1

54) chain B
residue 181
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:10745006, ECO:0007744|PDB:1DTW
source Swiss-Prot : SWS_FT_FI1

55) chain B
residue 183
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:10745006, ECO:0007744|PDB:1DTW
source Swiss-Prot : SWS_FT_FI1

56) chain A
residue 193
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10745006, ECO:0007744|PDB:1DTW
source Swiss-Prot : SWS_FT_FI1

57) chain A
residue 194
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:10745006, ECO:0007744|PDB:1DTW
source Swiss-Prot : SWS_FT_FI1

58) chain A
residue 195
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:10745006, ECO:0007744|PDB:1DTW
source Swiss-Prot : SWS_FT_FI1

59) chain A
residue 220
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:10745006, ECO:0007744|PDB:1DTW
source Swiss-Prot : SWS_FT_FI1

60) chain A
residue 222
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:10745006, ECO:0007744|PDB:1DTW
source Swiss-Prot : SWS_FT_FI1

61) chain A
residue 224
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:10745006, ECO:0007744|PDB:1DTW
source Swiss-Prot : SWS_FT_FI1

62) chain B
residue 102
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:10745006, ECO:0007744|PDB:1DTW
source Swiss-Prot : SWS_FT_FI1

63) chain B
residue 128
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:10745006, ECO:0007744|PDB:1DTW
source Swiss-Prot : SWS_FT_FI1

64) chain B
residue 130
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:10745006, ECO:0007744|PDB:1DTW
source Swiss-Prot : SWS_FT_FI1

65) chain B
residue 182
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:Q6P3A8
source Swiss-Prot : SWS_FT_FI2

66) chain B
residue 191
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI3


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