eF-site ID 5f95-AB
PDB Code 5f95
Chain A, B

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Title Crystal structure of GSK3b in complex with Compound 18: 2-[(cyclopropylcarbonyl)amino]-N-(4-phenylpyridin-3-yl)pyridine-4-carboxamide
Classification TRANSFERASE/TRANSFERASE INHIBITOR
Compound Glycogen synthase kinase-3 beta
Source Homo sapiens (Human) (GSK3B_HUMAN)
Sequence A:  KVTTVVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQAKL
CDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYF
FYSSGEKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPV
IYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAV
LKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYT
SSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGT
PTREQIREMNPNFKFPQIKAHPWTKVFRPRTPPEAIALCS
RLLEYTPTARLTPLEACAHSFFDELRDPNVKLPNGRDTPA
LFNFTTQELSSNPPLATILIPPHAR
B:  KVTTVVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQAKL
CDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYF
FYSSGEKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPV
IYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAV
LKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYT
SSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGT
PTREQIREMNPNPWTKVFRPRTPPEAIALCSRLLEYTPTA
RLTPLEACAHSFFDELRDPNVKLPNGRDTPALFNFTTQEL
SSNPPLATILIPPHARIQ
Description


Functional site

1) chain A
residue 85
type
sequence K
description binding site for residue 3UP A 401
source : AC1

2) chain A
residue 132
type
sequence L
description binding site for residue 3UP A 401
source : AC1

3) chain A
residue 133
type
sequence D
description binding site for residue 3UP A 401
source : AC1

4) chain A
residue 134
type
sequence Y
description binding site for residue 3UP A 401
source : AC1

5) chain A
residue 135
type
sequence V
description binding site for residue 3UP A 401
source : AC1

6) chain A
residue 185
type
sequence Q
description binding site for residue 3UP A 401
source : AC1

7) chain A
residue 188
type
sequence L
description binding site for residue 3UP A 401
source : AC1

8) chain A
residue 200
type
sequence D
description binding site for residue 3UP A 401
source : AC1

9) chain B
residue 83
type
sequence A
description binding site for residue 3UP B 401
source : AC2

10) chain B
residue 85
type
sequence K
description binding site for residue 3UP B 401
source : AC2

11) chain B
residue 132
type
sequence L
description binding site for residue 3UP B 401
source : AC2

12) chain B
residue 133
type
sequence D
description binding site for residue 3UP B 401
source : AC2

13) chain B
residue 134
type
sequence Y
description binding site for residue 3UP B 401
source : AC2

14) chain B
residue 135
type
sequence V
description binding site for residue 3UP B 401
source : AC2

15) chain B
residue 188
type
sequence L
description binding site for residue 3UP B 401
source : AC2

16) chain B
residue 199
type
sequence C
description binding site for residue 3UP B 401
source : AC2

17) chain B
residue 200
type
sequence D
description binding site for residue 3UP B 401
source : AC2

18) chain A
residue 62-86
type prosite
sequence IGNGSFGVVYQAKLCDSGELVAIKK
description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGNGSFGVVYqAklcdsgelv.........AIKK
source prosite : PS00107

19) chain A
residue 177-189
type prosite
sequence ICHRDIKPQNLLL
description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IcHrDIKpqNLLL
source prosite : PS00108

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

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

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

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

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

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

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


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