eF-site ID 6hk3-B
PDB Code 6hk3
Chain B

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Title Crystal structure of GSK-3B in complex with pyrazine inhibitor C44
Classification TRANSFERASE
Compound Glycogen synthase kinase-3 beta
Source (6HK3)
Sequence B:  SKVTTVVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQAK
LCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRY
FFYSSGEKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLP
VIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTA
VLKLCDFGSAKQLVRGEPNVSXICSRYYRAPELIFGATDY
TSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLG
TPTREQIREMNPNYTEFKFPQIKAHPWTKVFRPRTPPEAI
ALCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLPNGR
DTPALFNFTTQELSSNPPLATILIPPHARI
Description


Functional site

1) chain B
residue 290
type
sequence E
description binding site for residue GOL A 403
source : AC3

2) chain B
residue 83
type
sequence A
description binding site for residue G8B B 401
source : AC8

3) chain B
residue 85
type
sequence K
description binding site for residue G8B B 401
source : AC8

4) chain B
residue 110
type
sequence V
description binding site for residue G8B B 401
source : AC8

5) chain B
residue 133
type
sequence D
description binding site for residue G8B B 401
source : AC8

6) chain B
residue 134
type
sequence Y
description binding site for residue G8B B 401
source : AC8

7) chain B
residue 135
type
sequence V
description binding site for residue G8B B 401
source : AC8

8) chain B
residue 136
type
sequence P
description binding site for residue G8B B 401
source : AC8

9) chain B
residue 141
type
sequence R
description binding site for residue G8B B 401
source : AC8

10) chain B
residue 188
type
sequence L
description binding site for residue G8B B 401
source : AC8

11) chain B
residue 200
type
sequence D
description binding site for residue G8B B 401
source : AC8

12) chain B
residue 96
type
sequence R
description binding site for residue MLI B 402
source : AC9

13) chain B
residue 180
type
sequence R
description binding site for residue MLI B 402
source : AC9

14) chain B
residue 205
type
sequence K
description binding site for residue MLI B 402
source : AC9

15) chain B
residue 213
type
sequence N
description binding site for residue MLI B 402
source : AC9

16) chain B
residue 214
type
sequence V
description binding site for residue MLI B 402
source : AC9

17) chain B
residue 56
type
sequence Y
description binding site for residue GOL B 403
source : AD1

18) chain B
residue 86
type
sequence K
description binding site for residue GOL B 403
source : AD1

19) chain B
residue 129
type
sequence N
description binding site for residue GOL B 403
source : AD1

20) chain B
residue 106
type
sequence H
description binding site for residue CL B 404
source : AD2

21) chain B
residue 366
type
sequence E
description binding site for residue CL B 404
source : AD2

22) chain B
residue 157
type
sequence Y
description binding site for residue DMS B 405
source : AD3

23) chain B
residue 161
type
sequence Y
description binding site for residue DMS B 405
source : AD3

24) chain B
residue 85
type BINDING
sequence K
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:17050006
source Swiss-Prot : SWS_FT_FI3

25) chain B
residue 181
type ACT_SITE
sequence D
description Proton acceptor
source Swiss-Prot : SWS_FT_FI1

26) chain B
residue 62
type BINDING
sequence I
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
source Swiss-Prot : SWS_FT_FI2

27) chain B
residue 216
type MOD_RES
sequence X
description Phosphotyrosine => ECO:0000269|PubMed:12554650, ECO:0000269|PubMed:25169422
source Swiss-Prot : SWS_FT_FI4


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