eF-site ID 3x0c-AB
PDB Code 3x0c
Chain A, B

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Title Crystal structure of PIP4KIIBETA I368A 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
TRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKD
NDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYS
LLVGIHDVDRAEQEEMEVEERAEDGPGEFDPSVDVYAMKS
HESSPKKEVYFMAIADILTTVNPEQYSKRFNEFMSNILT
B:  VKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFK
AYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGI
DDQDYQNSVTRSAPINRFLTTYDRRFVIKTVSSEDVAEMH
NILKKYHQFIVECHGNTLLPQFLGMYRLTVDGVETYMVVT
RNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDN
DFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSL
LVGIHDVDRAEQFGPGEFDPSVDVYAMKSHESSPKKEVYF
MAIADILTPEQYSKRFNEFMSNILT
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 148
type
sequence V
description BINDING SITE FOR RESIDUE 5GP A 501
source : AC1

3) chain A
residue 150
type
sequence K
description BINDING SITE FOR RESIDUE 5GP A 501
source : AC1

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

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

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

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

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

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

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

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

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

13) chain A
residue 157
type
sequence V
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 154
type
sequence S
description BINDING SITE FOR RESIDUE 5GP A 503
source : AC3

18) chain A
residue 155
type
sequence E
description BINDING SITE FOR RESIDUE 5GP A 503
source : AC3

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

20) chain A
residue 293
type
sequence Q
description BINDING SITE FOR RESIDUE 5GP B 501
source : AC4

21) chain A
residue 297
type
sequence E
description BINDING SITE FOR RESIDUE 5GP B 501
source : AC4

22) chain B
residue 72
type
sequence K
description BINDING SITE FOR RESIDUE 5GP B 501
source : AC4

23) chain B
residue 96
type
sequence K
description BINDING SITE FOR RESIDUE 5GP B 501
source : AC4

24) chain B
residue 98
type
sequence Y
description BINDING SITE FOR RESIDUE 5GP B 501
source : AC4

25) chain B
residue 154
type
sequence S
description BINDING SITE FOR RESIDUE 5GP B 501
source : AC4

26) chain B
residue 157
type
sequence V
description BINDING SITE FOR RESIDUE 5GP B 501
source : AC4

27) chain B
residue 158
type
sequence A
description BINDING SITE FOR RESIDUE 5GP B 501
source : AC4

28) chain B
residue 161
type
sequence H
description BINDING SITE FOR RESIDUE 5GP B 501
source : AC4

29) chain B
residue 188
type
sequence R
description BINDING SITE FOR RESIDUE 5GP B 501
source : AC4

30) chain B
residue 197
type
sequence Y
description BINDING SITE FOR RESIDUE 5GP B 501
source : AC4

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

46) 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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