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

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Title Crystal structure of PIP4KIIBETA
Classification TRANSFERASE
Compound Phosphatidylinositol 5-phosphate 4-kinase type-2 beta
Source Homo sapiens (Human) (PI42B_HUMAN)
Sequence A:  KVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDF
KAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFG
IDDQDYQNSVTRSAPINSTRFLTTYDRRFVIKTVSSEDVA
EMHNILKKYHQFIVECHGNTLLPQFLGMYRLTVDGVETYM
VVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTF
KDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMD
YSLLVGIHDVDRAEQEEMEVEERAEDEGPGEFDPSVDVYA
MKSHESSPKKEVYFMAIIDILTTVNPEQYSKRFNEFMSNI
LT
B:  KVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDF
KAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFG
IDDQDYQNSVTRSAPINRFLTTYDRRFVIKTVSSEDVAEM
HNILKKYHQFIVECHGNTLLPQFLGMYRLTVDGVETYMVV
TRNVFSHRLTVHRKYDLKGSVAREASDKEKAKDLPTFKDN
DFLNELHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVG
IHDVDRAEQFFGPGEFDPSVDVYAMKSHESSPKKEVYFMA
IIDILTTVNPEQYSKRFNEFMSNILT
Description


Functional site

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

16) 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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