eF-site ID 1yve-L
PDB Code 1yve
Chain L

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Title ACETOHYDROXY ACID ISOMEROREDUCTASE COMPLEXED WITH NADPH, MAGNESIUM AND INHIBITOR IPOHA (N-HYDROXY-N-ISOPROPYLOXAMATE)
Classification OXIDOREDUCTASE
Compound ACETOHYDROXY ACID ISOMEROREDUCTASE
Source null (ILV5_SPIOL)
Sequence L:  ATTFDFDSSVFKKEKVTLSGHDEYIVRGGRNLFPLLPDAF
KGIKQIGVIGWGSQAPAQAQNLKDSLTEAKSDVVVKIGLR
KGSNSFAEARAAGFSEENGTLGDMWETISGSDLVLLLISD
SAQADNYEKVFSHMKPNSILGLSHGFLLGHLQSLGQDFPK
NISVIAVCPKGMGPSVRRLYVQGKEVNGAGINSSFAVHQD
VDGRATDVALGWSIALGSPFTFATTLEQEYKSDIFGERGI
LLGAVHGIVECLFRRYTESGMSEDLAYKNTVECITGVISK
TISTKGMLALYNSLSEEGKKDFQAAYSASYYPSMDILYEC
YEDVASGSEIRSVVLAGRRFYEKEGLPAFPMGKIDQTRMW
KVGEKVRSVRPAGDLGPLYPFTAGVYVALMMAQIEILRKK
GHSYSEIINESVIEAVDSLNPFMHARGVSFMVDNCSTTAR
LGSRKWAPRFDYILSQQALVAVDNGAPINQDLISNFLSDP
VHEAIGVCAQLRPSVDISVTADADFVRPELRQA
Description


Functional site

1) chain L
residue 315
type
sequence D
description BINDING SITE FOR RESIDUE MG L 601
source : BC1

2) chain L
residue 319
type
sequence E
description BINDING SITE FOR RESIDUE MG L 601
source : BC1

3) chain L
residue 315
type
sequence D
description BINDING SITE FOR RESIDUE MG L 602
source : BC2

4) chain L
residue 132
type
sequence G
description BINDING SITE FOR RESIDUE NDP K 605
source : BC7

5) chain L
residue 133
type
sequence W
description BINDING SITE FOR RESIDUE NDP K 605
source : BC7

6) chain L
residue 134
type
sequence G
description BINDING SITE FOR RESIDUE NDP K 605
source : BC7

7) chain L
residue 135
type
sequence S
description BINDING SITE FOR RESIDUE NDP K 605
source : BC7

8) chain L
residue 136
type
sequence Q
description BINDING SITE FOR RESIDUE NDP K 605
source : BC7

9) chain L
residue 162
type
sequence R
description BINDING SITE FOR RESIDUE NDP K 605
source : BC7

10) chain L
residue 165
type
sequence S
description BINDING SITE FOR RESIDUE NDP K 605
source : BC7

11) chain L
residue 167
type
sequence S
description BINDING SITE FOR RESIDUE NDP K 605
source : BC7

12) chain L
residue 199
type
sequence L
description BINDING SITE FOR RESIDUE NDP K 605
source : BC7

13) chain L
residue 200
type
sequence I
description BINDING SITE FOR RESIDUE NDP K 605
source : BC7

14) chain L
residue 201
type
sequence S
description BINDING SITE FOR RESIDUE NDP K 605
source : BC7

15) chain L
residue 202
type
sequence D
description BINDING SITE FOR RESIDUE NDP K 605
source : BC7

16) chain L
residue 204
type
sequence A
description BINDING SITE FOR RESIDUE NDP K 605
source : BC7

17) chain L
residue 205
type
sequence Q
description BINDING SITE FOR RESIDUE NDP K 605
source : BC7

18) chain L
residue 225
type
sequence S
description BINDING SITE FOR RESIDUE NDP K 605
source : BC7

19) chain L
residue 226
type
sequence H
description BINDING SITE FOR RESIDUE NDP K 605
source : BC7

20) chain L
residue 251
type
sequence P
description BINDING SITE FOR RESIDUE NDP K 605
source : BC7

21) chain L
residue 253
type
sequence G
description BINDING SITE FOR RESIDUE NDP K 605
source : BC7

22) chain L
residue 254
type
sequence M
description BINDING SITE FOR RESIDUE NDP K 605
source : BC7

23) chain L
residue 255
type
sequence G
description BINDING SITE FOR RESIDUE NDP K 605
source : BC7

24) chain L
residue 517
type
sequence C
description BINDING SITE FOR RESIDUE NDP K 605
source : BC7

25) chain L
residue 518
type
sequence S
description BINDING SITE FOR RESIDUE NDP K 605
source : BC7

26) chain L
residue 519
type
sequence T
description BINDING SITE FOR RESIDUE NDP K 605
source : BC7

27) chain L
residue 589
type
sequence R
description BINDING SITE FOR RESIDUE NDP K 605
source : BC7

28) chain L
residue 253
type
sequence G
description BINDING SITE FOR RESIDUE HIO L 603
source : CC1

29) chain L
residue 254
type
sequence M
description BINDING SITE FOR RESIDUE HIO L 603
source : CC1

30) chain L
residue 315
type
sequence D
description BINDING SITE FOR RESIDUE HIO L 603
source : CC1

31) chain L
residue 319
type
sequence E
description BINDING SITE FOR RESIDUE HIO L 603
source : CC1

32) chain L
residue 496
type
sequence E
description BINDING SITE FOR RESIDUE HIO L 603
source : CC1

33) chain L
residue 501
type
sequence L
description BINDING SITE FOR RESIDUE HIO L 603
source : CC1

34) chain L
residue 517
type
sequence C
description BINDING SITE FOR RESIDUE HIO L 603
source : CC1

35) chain L
residue 518
type
sequence S
description BINDING SITE FOR RESIDUE HIO L 603
source : CC1

36) chain L
residue 521
type
sequence A
description BINDING SITE FOR RESIDUE HIO L 603
source : CC1

37) chain L
residue 226
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

38) chain L
residue 129
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:10739911, ECO:0000269|PubMed:9218783
source Swiss-Prot : SWS_FT_FI2

39) chain L
residue 162
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:10739911, ECO:0000269|PubMed:9218783
source Swiss-Prot : SWS_FT_FI2

40) chain L
residue 201
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:10739911, ECO:0000269|PubMed:9218783
source Swiss-Prot : SWS_FT_FI2

41) chain L
residue 315
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01198
source Swiss-Prot : SWS_FT_FI3

42) chain L
residue 319
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01198
source Swiss-Prot : SWS_FT_FI3

43) chain L
residue 492
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01198
source Swiss-Prot : SWS_FT_FI3

44) chain L
residue 496
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01198
source Swiss-Prot : SWS_FT_FI3

45) chain L
residue 518
type BINDING
sequence S
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01198
source Swiss-Prot : SWS_FT_FI3

46) chain L
residue 252
type catalytic
sequence K
description 890
source MCSA : MCSA4

47) chain L
residue 315
type catalytic
sequence D
description 890
source MCSA : MCSA4

48) chain L
residue 319
type catalytic
sequence E
description 890
source MCSA : MCSA4


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