eF-site ID 3lc6-AB
PDB Code 3lc6
Chain A, B

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Title The alternative conformation structure of isocitrate dehydrogenase kinase/phosphatase from E. Coli
Classification TRANSFERASE, HYDROLASE
Compound Isocitrate dehydrogenase kinase/phosphatase
Source null (ACEK_ECO5E)
Sequence A:  RGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHA
VQQAMKNRIHLYDHHVGLVVEQLRCITNGQSTDAEFLLRV
KEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLF
IFSSQPERRFRTIPRPLAKDFHPDHGWESLLMRVISDLPL
RLHWQNKSRDIHYIIRHLTETLSKSHLQVANELFYRNKAA
WLVGKLITPSGTLPFLLPIHQTDDGELFIDTCLTTTAEAS
IVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAI
GCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFT
LPGFDRVFKVIKDKFAPQKEMSAAHVRACYQLVKEHDRVG
RMADTQEFENFVLEKRHISPALMELLLQEAAEKITDLGEQ
IVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQ
LAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNF
RDIPSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADY
WRALQNRIREGHVEDVYAYRRRQRFSV
B:  PRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWH
AVQQAMKNRIHLYDHHVGLVVEQLRCITNGQSTDAEFLLR
VKEHYTRLLPDYPRFEIAESFFNSVYCRLDHRSLTPERLF
IFSSQPTIPRPLAKDFHPDHGWESLLMRVISDLPLRLHWQ
NKSRDIHYIIRHLTETLGPENLSKSHLQVANELFYRNKAA
WLVGKLITPSGTLPFLLPIHQTDDGELFIDTCLTTTAEAS
IVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAI
GCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFT
LPGFDRVFKVIKDKFAHVRACYQLVKEHDRVGRMADTQEF
ENFVLEKRHISPALMELLLQEAAEKITDLGEQIVIRHLYI
ERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFP
GDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIGDVFP
EEFRHWLCADPRIGPLFEEMHADLFRADYWRALQNRIREG
HVEDVYAYRRRQRFSVRYG
Description


Functional site

1) chain A
residue 316
type
sequence P
description BINDING SITE FOR RESIDUE ADP A 1762
source : AC1

2) chain A
residue 318
type
sequence I
description BINDING SITE FOR RESIDUE ADP A 1762
source : AC1

3) chain A
residue 320
type
sequence G
description BINDING SITE FOR RESIDUE ADP A 1762
source : AC1

4) chain A
residue 321
type
sequence M
description BINDING SITE FOR RESIDUE ADP A 1762
source : AC1

5) chain A
residue 322
type
sequence V
description BINDING SITE FOR RESIDUE ADP A 1762
source : AC1

6) chain A
residue 323
type
sequence M
description BINDING SITE FOR RESIDUE ADP A 1762
source : AC1

7) chain A
residue 325
type
sequence V
description BINDING SITE FOR RESIDUE ADP A 1762
source : AC1

8) chain A
residue 334
type
sequence V
description BINDING SITE FOR RESIDUE ADP A 1762
source : AC1

9) chain A
residue 336
type
sequence K
description BINDING SITE FOR RESIDUE ADP A 1762
source : AC1

10) chain A
residue 416
type
sequence E
description BINDING SITE FOR RESIDUE ADP A 1762
source : AC1

11) chain A
residue 417
type
sequence R
description BINDING SITE FOR RESIDUE ADP A 1762
source : AC1

12) chain A
residue 419
type
sequence M
description BINDING SITE FOR RESIDUE ADP A 1762
source : AC1

13) chain A
residue 421
type
sequence P
description BINDING SITE FOR RESIDUE ADP A 1762
source : AC1

14) chain A
residue 462
type
sequence N
description BINDING SITE FOR RESIDUE ADP A 1762
source : AC1

15) chain A
residue 474
type
sequence Y
description BINDING SITE FOR RESIDUE ADP A 1762
source : AC1

16) chain A
residue 475
type
sequence D
description BINDING SITE FOR RESIDUE ADP A 1762
source : AC1

17) chain A
residue 461
type
sequence K
description BINDING SITE FOR RESIDUE MG A 579
source : AC2

18) chain A
residue 462
type
sequence N
description BINDING SITE FOR RESIDUE MG A 579
source : AC2

19) chain A
residue 475
type
sequence D
description BINDING SITE FOR RESIDUE MG A 579
source : AC2

20) chain B
residue 101
type
sequence S
description BINDING SITE FOR RESIDUE AMP B 1604
source : AC3

21) chain B
residue 104
type
sequence N
description BINDING SITE FOR RESIDUE AMP B 1604
source : AC3

22) chain B
residue 105
type
sequence S
description BINDING SITE FOR RESIDUE AMP B 1604
source : AC3

23) chain B
residue 113
type
sequence H
description BINDING SITE FOR RESIDUE AMP B 1604
source : AC3

24) chain B
residue 123
type
sequence I
description BINDING SITE FOR RESIDUE AMP B 1604
source : AC3

25) chain B
residue 291
type
sequence K
description BINDING SITE FOR RESIDUE AMP B 1604
source : AC3

26) chain B
residue 294
type
sequence K
description BINDING SITE FOR RESIDUE AMP B 1604
source : AC3

27) chain B
residue 295
type
sequence T
description BINDING SITE FOR RESIDUE AMP B 1604
source : AC3

28) chain B
residue 375
type
sequence F
description BINDING SITE FOR RESIDUE AMP B 1604
source : AC3

29) chain B
residue 377
type
sequence N
description BINDING SITE FOR RESIDUE AMP B 1604
source : AC3

30) chain A
residue 371
type ACT_SITE
sequence D
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00747
source Swiss-Prot : SWS_FT_FI1

31) chain B
residue 371
type ACT_SITE
sequence D
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00747
source Swiss-Prot : SWS_FT_FI1

32) chain A
residue 370
type ACT_SITE
sequence A
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00747
source Swiss-Prot : SWS_FT_FI1

33) chain B
residue 370
type ACT_SITE
sequence A
description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00747
source Swiss-Prot : SWS_FT_FI1

34) chain B
residue 314
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_00747
source Swiss-Prot : SWS_FT_FI2

35) chain B
residue 335
type BINDING
sequence F
description BINDING => ECO:0000255|HAMAP-Rule:MF_00747
source Swiss-Prot : SWS_FT_FI2

36) chain A
residue 315
type BINDING
sequence A
description BINDING => ECO:0000255|HAMAP-Rule:MF_00747
source Swiss-Prot : SWS_FT_FI2

37) chain A
residue 336
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_00747
source Swiss-Prot : SWS_FT_FI2

38) chain B
residue 315
type BINDING
sequence A
description BINDING => ECO:0000255|HAMAP-Rule:MF_00747
source Swiss-Prot : SWS_FT_FI2

39) chain B
residue 336
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_00747
source Swiss-Prot : SWS_FT_FI2

40) chain A
residue 314
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_00747
source Swiss-Prot : SWS_FT_FI2

41) chain A
residue 335
type BINDING
sequence F
description BINDING => ECO:0000255|HAMAP-Rule:MF_00747
source Swiss-Prot : SWS_FT_FI2


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