eF-site ID 3x0b-B
PDB Code 3x0b
Chain B

click to enlarge
Title Crystal structure of PIP4KIIBETA I368A complex with AMP
Classification TRANSFERASE
Compound Phosphatidylinositol 5-phosphate 4-kinase type-2 beta
Source Homo sapiens (Human) (PI42B_HUMAN)
Sequence B:  KVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDF
KAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFG
IDDQDYQNSVTRSAPINRFLTTYDRRFVIKTVSSEDVAEM
HNILKKYHQFIVECHGNTLLPQFLGMYRLTVDGVETYMVV
TRNVFSHRLTVHRKYDLKAREASDKEKAKDLPTFKDNDFL
NEGQKHVSKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDV
DRAEQRFFGPGEFDPSVDVYAMKSHESSPKKEVYFMAIAD
ILTNPEQYSKRFNEFMSNILT
Description


Functional site

1) chain B
residue 96
type
sequence K
description BINDING SITE FOR RESIDUE AMP A 502
source : AC2

2) chain B
residue 98
type
sequence Y
description BINDING SITE FOR RESIDUE AMP A 502
source : AC2

3) chain B
residue 154
type
sequence S
description BINDING SITE FOR RESIDUE AMP A 502
source : AC2

4) chain B
residue 157
type
sequence V
description BINDING SITE FOR RESIDUE AMP A 502
source : AC2

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

6) chain B
residue 161
type
sequence H
description BINDING SITE FOR RESIDUE AMP A 502
source : AC2

7) chain B
residue 188
type
sequence R
description BINDING SITE FOR RESIDUE AMP A 502
source : AC2

8) chain B
residue 197
type
sequence Y
description BINDING SITE FOR RESIDUE AMP A 502
source : AC2

9) chain B
residue 139
type
sequence F
description BINDING SITE FOR RESIDUE AMP B 501
source : AC4

10) chain B
residue 148
type
sequence V
description BINDING SITE FOR RESIDUE AMP B 501
source : AC4

11) chain B
residue 150
type
sequence K
description BINDING SITE FOR RESIDUE AMP B 501
source : AC4

12) chain B
residue 203
type
sequence N
description BINDING SITE FOR RESIDUE AMP B 501
source : AC4

13) chain B
residue 204
type
sequence V
description BINDING SITE FOR RESIDUE AMP B 501
source : AC4

14) chain B
residue 205
type
sequence F
description BINDING SITE FOR RESIDUE AMP B 501
source : AC4

15) chain B
residue 216
type
sequence D
description BINDING SITE FOR RESIDUE AMP B 501
source : AC4

16) chain B
residue 282
type
sequence L
description BINDING SITE FOR RESIDUE AMP B 501
source : AC4

17) chain B
residue 369
type
sequence D
description BINDING SITE FOR RESIDUE AMP B 501
source : AC4

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

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

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

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

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

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

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

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


Display surface

Download
Links