eF-site ID 1cwu-B
PDB Code 1cwu
Chain B

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Title BRASSICA NAPUS ENOYL ACP REDUCTASE A138G MUTANT COMPLEXED WITH NAD+ AND THIENODIAZABORINE
Classification OXIDOREDUCTASE
Compound ENOYL ACP REDUCTASE
Source Brassica napus (Rape) (FABI_BRANA)
Sequence B:  LPIDLRGKRAFIAGIADDNGYGWAVAKSLAAAGAEILVGT
WVPALNIFETSLRRGKFDQSRVLPDGSLMEIKKVYPLDAV
FDNPEDVPEDVKANKRYAGSSNWTVQEAAECVRQDFGSID
ILVHSLGNGPEVSKPLLETSRKGYLAAISASSYSFVSLLS
HFLPIMNPGGASISLTYIASERIIPGYGGGMSSAKAALES
DTRVLAFEAGRKQNIRVNTISAGPLGSRAAKAIGFIDTMI
EYSYNNAPIQKTLTADEVGNAAAFLVSPLASAITGATIYV
DNGLNSMGVALDSPVF
Description


Functional site

1) chain B
residue 25
type
sequence G
description BINDING SITE FOR RESIDUE NAD B 503
source : AC3

2) chain B
residue 26
type
sequence I
description BINDING SITE FOR RESIDUE NAD B 503
source : AC3

3) chain B
residue 27
type
sequence A
description BINDING SITE FOR RESIDUE NAD B 503
source : AC3

4) chain B
residue 31
type
sequence G
description BINDING SITE FOR RESIDUE NAD B 503
source : AC3

5) chain B
residue 32
type
sequence Y
description BINDING SITE FOR RESIDUE NAD B 503
source : AC3

6) chain B
residue 52
type
sequence W
description BINDING SITE FOR RESIDUE NAD B 503
source : AC3

7) chain B
residue 89
type
sequence D
description BINDING SITE FOR RESIDUE NAD B 503
source : AC3

8) chain B
residue 90
type
sequence A
description BINDING SITE FOR RESIDUE NAD B 503
source : AC3

9) chain B
residue 136
type
sequence S
description BINDING SITE FOR RESIDUE NAD B 503
source : AC3

10) chain B
residue 137
type
sequence L
description BINDING SITE FOR RESIDUE NAD B 503
source : AC3

11) chain B
residue 138
type
sequence G
description BINDING SITE FOR RESIDUE NAD B 503
source : AC3

12) chain B
residue 186
type
sequence L
description BINDING SITE FOR RESIDUE NAD B 503
source : AC3

13) chain B
residue 187
type
sequence T
description BINDING SITE FOR RESIDUE NAD B 503
source : AC3

14) chain B
residue 206
type
sequence K
description BINDING SITE FOR RESIDUE NAD B 503
source : AC3

15) chain B
residue 233
type
sequence A
description BINDING SITE FOR RESIDUE NAD B 503
source : AC3

16) chain B
residue 234
type
sequence G
description BINDING SITE FOR RESIDUE NAD B 503
source : AC3

17) chain B
residue 235
type
sequence P
description BINDING SITE FOR RESIDUE NAD B 503
source : AC3

18) chain B
residue 236
type
sequence L
description BINDING SITE FOR RESIDUE NAD B 503
source : AC3

19) chain B
residue 238
type
sequence S
description BINDING SITE FOR RESIDUE NAD B 503
source : AC3

20) chain B
residue 240
type
sequence A
description BINDING SITE FOR RESIDUE NAD B 503
source : AC3

21) chain B
residue 241
type
sequence A
description BINDING SITE FOR RESIDUE NAD B 503
source : AC3

22) chain B
residue 138
type
sequence G
description BINDING SITE FOR RESIDUE TDB B 504
source : AC4

23) chain B
residue 198
type
sequence Y
description BINDING SITE FOR RESIDUE TDB B 504
source : AC4

24) chain B
residue 202
type
sequence M
description BINDING SITE FOR RESIDUE TDB B 504
source : AC4

25) chain B
residue 206
type
sequence K
description BINDING SITE FOR RESIDUE TDB B 504
source : AC4

26) chain B
residue 240
type
sequence A
description BINDING SITE FOR RESIDUE TDB B 504
source : AC4

27) chain B
residue 241
type
sequence A
description BINDING SITE FOR RESIDUE TDB B 504
source : AC4

28) chain B
residue 244
type
sequence I
description BINDING SITE FOR RESIDUE TDB B 504
source : AC4

29) chain B
residue 188
type ACT_SITE
sequence Y
description Proton acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

30) chain B
residue 198
type ACT_SITE
sequence Y
description Proton acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

31) chain B
residue 89
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:10521472, ECO:0000269|PubMed:10610777, ECO:0000269|PubMed:8535786
source Swiss-Prot : SWS_FT_FI2

32) chain B
residue 136
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:10521472, ECO:0000269|PubMed:10610777, ECO:0000269|PubMed:8535786
source Swiss-Prot : SWS_FT_FI2

33) chain B
residue 186
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:10521472, ECO:0000269|PubMed:10610777, ECO:0000269|PubMed:8535786
source Swiss-Prot : SWS_FT_FI2

34) chain B
residue 206
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:10521472, ECO:0000269|PubMed:10610777, ECO:0000269|PubMed:8535786
source Swiss-Prot : SWS_FT_FI2

35) chain B
residue 236
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:10521472, ECO:0000269|PubMed:10610777, ECO:0000269|PubMed:8535786
source Swiss-Prot : SWS_FT_FI2

36) chain B
residue 25
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:10521472, ECO:0000269|PubMed:10610777, ECO:0000269|PubMed:8535786
source Swiss-Prot : SWS_FT_FI2

37) chain B
residue 32
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:10521472, ECO:0000269|PubMed:10610777, ECO:0000269|PubMed:8535786
source Swiss-Prot : SWS_FT_FI2


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