eF-site ID 3x02-AB
PDB Code 3x02
Chain A, B

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Title Crystal structure of PIP4KIIBETA complex with GMP
Classification TRANSFERASE
Compound Phosphatidylinositol 5-phosphate 4-kinase type-2 beta
Source Homo sapiens (Human) (PI42B_HUMAN)
Sequence A:  KVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDF
KAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFG
IDDQDYQNSVTRSAPINRFLTTYDRRFVIKTVSSEDVAEM
HNILKKYHQFIVECHGNTLLPQFLGMYRLTVDGVETYMVV
TRNVFSHRLTVHRKYDLKGSTAREASDKEKAKDLPTFKDN
DFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSL
LVGIHDVDRAEQEEMEVEERAEDPGEFDPSVDVYAMKSHE
SSPKKEVYFMAIIDILTPVNPEQYSKRFNEFMSNILT
B:  VKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFK
AYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGI
DDQDYQNSVTRSAPINRFLTTYDRRFVIKTVSSEDVAEMH
NILKKYHQFIVECHGNTLLPQFLGMYRLTVDGVETYMVVT
RNVFSHRLTVHRKYDLKGSVAREASDKEKAKDLPTFKDND
FLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLL
VGIHDVDRAEQFGPGEFDPSVDVYAMKSHESSPKKEVYFM
AIIDILTPEQYSKRFNEFMSNILT
Description


Functional site

1) chain A
residue 139
type
sequence F
description BINDING SITE FOR RESIDUE 5GP A 501
source : AC1

2) chain A
residue 203
type
sequence N
description BINDING SITE FOR RESIDUE 5GP A 501
source : AC1

3) chain A
residue 204
type
sequence V
description BINDING SITE FOR RESIDUE 5GP A 501
source : AC1

4) chain A
residue 205
type
sequence F
description BINDING SITE FOR RESIDUE 5GP A 501
source : AC1

5) chain A
residue 214
type
sequence K
description BINDING SITE FOR RESIDUE 5GP A 501
source : AC1

6) chain A
residue 237
type
sequence T
description BINDING SITE FOR RESIDUE 5GP A 501
source : AC1

7) chain A
residue 282
type
sequence L
description BINDING SITE FOR RESIDUE 5GP A 501
source : AC1

8) chain A
residue 369
type
sequence D
description BINDING SITE FOR RESIDUE 5GP A 501
source : AC1

9) chain A
residue 96
type
sequence K
description BINDING SITE FOR RESIDUE 5GP A 502
source : AC2

10) chain A
residue 98
type
sequence Y
description BINDING SITE FOR RESIDUE 5GP A 502
source : AC2

11) chain A
residue 154
type
sequence S
description BINDING SITE FOR RESIDUE 5GP A 502
source : AC2

12) chain A
residue 157
type
sequence V
description BINDING SITE FOR RESIDUE 5GP A 502
source : AC2

13) chain A
residue 158
type
sequence A
description BINDING SITE FOR RESIDUE 5GP A 502
source : AC2

14) chain A
residue 161
type
sequence H
description BINDING SITE FOR RESIDUE 5GP A 502
source : AC2

15) chain A
residue 188
type
sequence R
description BINDING SITE FOR RESIDUE 5GP A 502
source : AC2

16) chain A
residue 197
type
sequence Y
description BINDING SITE FOR RESIDUE 5GP A 502
source : AC2

17) chain A
residue 293
type
sequence Q
description BINDING SITE FOR RESIDUE 5GP A 503
source : AC3

18) chain A
residue 297
type
sequence E
description BINDING SITE FOR RESIDUE 5GP A 503
source : AC3

19) chain A
residue 300
type
sequence E
description BINDING SITE FOR RESIDUE 5GP A 503
source : AC3

20) chain B
residue 96
type
sequence K
description BINDING SITE FOR RESIDUE 5GP A 503
source : AC3

21) chain B
residue 98
type
sequence Y
description BINDING SITE FOR RESIDUE 5GP A 503
source : AC3

22) chain B
residue 154
type
sequence S
description BINDING SITE FOR RESIDUE 5GP A 503
source : AC3

23) chain B
residue 157
type
sequence V
description BINDING SITE FOR RESIDUE 5GP A 503
source : AC3

24) chain B
residue 158
type
sequence A
description BINDING SITE FOR RESIDUE 5GP A 503
source : AC3

25) chain B
residue 161
type
sequence H
description BINDING SITE FOR RESIDUE 5GP A 503
source : AC3

26) chain B
residue 188
type
sequence R
description BINDING SITE FOR RESIDUE 5GP A 503
source : AC3

27) chain B
residue 197
type
sequence Y
description BINDING SITE FOR RESIDUE 5GP A 503
source : AC3

28) chain A
residue 158
type
sequence A
description BINDING SITE FOR RESIDUE 5GP A 504
source : AC4

29) chain B
residue 139
type
sequence F
description BINDING SITE FOR RESIDUE 5GP B 501
source : AC5

30) chain B
residue 148
type
sequence V
description BINDING SITE FOR RESIDUE 5GP B 501
source : AC5

31) chain B
residue 150
type
sequence K
description BINDING SITE FOR RESIDUE 5GP B 501
source : AC5

32) chain B
residue 203
type
sequence N
description BINDING SITE FOR RESIDUE 5GP B 501
source : AC5

33) chain B
residue 204
type
sequence V
description BINDING SITE FOR RESIDUE 5GP B 501
source : AC5

34) chain B
residue 205
type
sequence F
description BINDING SITE FOR RESIDUE 5GP B 501
source : AC5

35) chain B
residue 214
type
sequence K
description BINDING SITE FOR RESIDUE 5GP B 501
source : AC5

36) chain B
residue 237
type
sequence T
description BINDING SITE FOR RESIDUE 5GP B 501
source : AC5

37) chain B
residue 282
type
sequence L
description BINDING SITE FOR RESIDUE 5GP B 501
source : AC5

38) chain B
residue 369
type
sequence D
description BINDING SITE FOR RESIDUE 5GP B 501
source : AC5

39) chain A
residue 150
type catalytic
sequence K
description 662
source MCSA : MCSA1

40) chain A
residue 278
type catalytic
sequence D
description 662
source MCSA : MCSA1

41) chain B
residue 150
type catalytic
sequence K
description 662
source MCSA : MCSA2

42) chain B
residue 278
type catalytic
sequence D
description 662
source MCSA : MCSA2

43) chain A
residue 202
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:26774281, ECO:0007744|PDB:3X03
source Swiss-Prot : SWS_FT_FI1

44) chain B
residue 202
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:26774281, ECO:0007744|PDB:3X03
source Swiss-Prot : SWS_FT_FI1

45) chain A
residue 203
type BINDING
sequence N
description BINDING => ECO:0000305|PubMed:26774281, ECO:0007744|PDB:3X04
source Swiss-Prot : SWS_FT_FI2

46) chain A
residue 214
type BINDING
sequence K
description BINDING => ECO:0000305|PubMed:26774281, ECO:0007744|PDB:3X04
source Swiss-Prot : SWS_FT_FI2

47) chain A
residue 369
type BINDING
sequence D
description BINDING => ECO:0000305|PubMed:26774281, ECO:0007744|PDB:3X04
source Swiss-Prot : SWS_FT_FI2

48) chain B
residue 203
type BINDING
sequence N
description BINDING => ECO:0000305|PubMed:26774281, ECO:0007744|PDB:3X04
source Swiss-Prot : SWS_FT_FI2

49) chain B
residue 214
type BINDING
sequence K
description BINDING => ECO:0000305|PubMed:26774281, ECO:0007744|PDB:3X04
source Swiss-Prot : SWS_FT_FI2

50) chain B
residue 369
type BINDING
sequence D
description BINDING => ECO:0000305|PubMed:26774281, ECO:0007744|PDB:3X04
source Swiss-Prot : SWS_FT_FI2

51) chain A
residue 94
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P48426
source Swiss-Prot : SWS_FT_FI3

52) chain B
residue 94
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P48426
source Swiss-Prot : SWS_FT_FI3

53) chain A
residue 150
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4

54) chain B
residue 150
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4


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