eF-site ID 2bfd-B
PDB Code 2bfd
Chain 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 B:  AHFEYGQTQKMNLFQSVTSALDNSLAKDPTAVIFGEDVAF
GGVFRCTVGLRDKYGKDRVFNTPLCEQGIVGFGIGIAVTG
ATAIAEIQFADYIFPAFDQIVNEAAKYRYRSGDLFNCGSL
TIRSPWGCVGHGALYHSQSPEAFFAHCPGIKVVIPRSPFQ
AKGLLLSCIEDKNPCIFFEPKILYRAAAEEVPIEPYNIPL
SQAEVIQEGSDVTLVAWGTQVHVIREVASMAKEKLGVSCE
VIDLRTIIPWDVDTICKSVIKTGRLLISHEAPLTGGFASE
ISSTVQEECFLNLEAPISRVCGYDTPFPHIFEPFYIPDKW
KCYDALRKMINY
Description


Functional site

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

26) 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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