eF-site ID 2fju-AB
PDB Code 2fju
Chain A, B

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Title Activated Rac1 bound to its effector phospholipase C beta 2
Classification SIGNALING PROTEIN,APOPTOSIS/HYDROLASE
Compound Ras-related C3 botulinum toxin substrate 1
Source Homo sapiens (Human) (PLCB2_HUMAN)
Sequence A:  MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNY
SANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLI
CFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLR
DDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSAL
TQRGLKTVFDEAIRAVL
B:  PKVKAYLSQGERFIKWDDETTVASPVILRVDPKGYYLYWT
YQSKEMEFLDITSIRDTRFGKFAKMPKSQKLRDVFNMDFP
DNSFLLKTLTVVSGPDMVDLTFHNFVSYKENVGKAWAEDV
LALVKHPLTANASRSTFLDKILVKLKMQLNSEGKIPVKNF
FQMFPADRKRVEAALSACHLPKGKNDAINPEDFPEPVYKS
FLMSLCPRPEIDEIFTSYMTKEHLTKFINQKQRDQGLIDK
YEPSGQLSPEGMVWFLCGPENSVLAQDKLLLHHDMTQPLN
HYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELD
CWKGKPPDEEPIITHGFTMTTDIFFKEAIEAIAESAFKTS
PYPIILSFENHVDSPRQQAKMAEYCRTIFGDMLLTEPLEK
FPLKPGVPLPSPEDLRGKILIKNKKEESGNLDEEEIKKMQ
SDEGTAGLEVTAYEEMSSLVNYIQPTKFVSFEFSAQKNRS
YVISSFTELKAYDLLSKASVQFVDYNKRQMSRIYPKGTRM
DSSNYMPQMFWNAGCQMVALNFQTMDLPMQQNMAVFEFNG
QSGYLLKHEFMRRPTTLSITVISGQFLSERSVRTYVEVEL
FGLPGDPKRRYRTKLSPSTNSINPVWKEEPFVFEKILMPE
LASLRVAVMEEGNKFLGHRIIPINALNSGYHHLCLHSESN
MPLTMPALFIFLEMKD
Description


Functional site

1) chain A
residue 17
type
sequence T
description BINDING SITE FOR RESIDUE MG A 179
source : AC1

2) chain A
residue 33
type
sequence I
description BINDING SITE FOR RESIDUE MG A 179
source : AC1

3) chain A
residue 35
type
sequence T
description BINDING SITE FOR RESIDUE MG A 179
source : AC1

4) chain B
residue 328
type
sequence N
description BINDING SITE FOR RESIDUE CA B 1000
source : AC2

5) chain B
residue 357
type
sequence E
description BINDING SITE FOR RESIDUE CA B 1000
source : AC2

6) chain B
residue 359
type
sequence D
description BINDING SITE FOR RESIDUE CA B 1000
source : AC2

7) chain B
residue 408
type
sequence E
description BINDING SITE FOR RESIDUE CA B 1000
source : AC2

8) chain A
residue 12
type
sequence G
description BINDING SITE FOR RESIDUE GSP A 2466
source : AC3

9) chain A
residue 13
type
sequence A
description BINDING SITE FOR RESIDUE GSP A 2466
source : AC3

10) chain A
residue 14
type
sequence V
description BINDING SITE FOR RESIDUE GSP A 2466
source : AC3

11) chain A
residue 15
type
sequence G
description BINDING SITE FOR RESIDUE GSP A 2466
source : AC3

12) chain A
residue 16
type
sequence K
description BINDING SITE FOR RESIDUE GSP A 2466
source : AC3

13) chain A
residue 17
type
sequence T
description BINDING SITE FOR RESIDUE GSP A 2466
source : AC3

14) chain A
residue 18
type
sequence C
description BINDING SITE FOR RESIDUE GSP A 2466
source : AC3

15) chain A
residue 28
type
sequence F
description BINDING SITE FOR RESIDUE GSP A 2466
source : AC3

16) chain A
residue 32
type
sequence Y
description BINDING SITE FOR RESIDUE GSP A 2466
source : AC3

17) chain A
residue 35
type
sequence T
description BINDING SITE FOR RESIDUE GSP A 2466
source : AC3

18) chain A
residue 60
type
sequence G
description BINDING SITE FOR RESIDUE GSP A 2466
source : AC3

19) chain A
residue 116
type
sequence K
description BINDING SITE FOR RESIDUE GSP A 2466
source : AC3

20) chain A
residue 118
type
sequence D
description BINDING SITE FOR RESIDUE GSP A 2466
source : AC3

21) chain A
residue 119
type
sequence L
description BINDING SITE FOR RESIDUE GSP A 2466
source : AC3

22) chain A
residue 158
type
sequence S
description BINDING SITE FOR RESIDUE GSP A 2466
source : AC3

23) chain A
residue 159
type
sequence A
description BINDING SITE FOR RESIDUE GSP A 2466
source : AC3

24) chain A
residue 160
type
sequence L
description BINDING SITE FOR RESIDUE GSP A 2466
source : AC3

25) chain B
residue 327
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00270
source Swiss-Prot : SWS_FT_FI1

26) chain B
residue 374
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00270
source Swiss-Prot : SWS_FT_FI1

27) chain A
residue 60
type ACT_SITE
sequence G
description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00270
source Swiss-Prot : SWS_FT_FI1

28) chain B
residue 328
type BINDING
sequence N
description
source Swiss-Prot : SWS_FT_FI2

29) chain B
residue 357
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI2

30) chain B
residue 359
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI2

31) chain B
residue 408
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI2

32) chain A
residue 32
type MOD_RES
sequence Y
description (Microbial infection) O-AMP-tyrosine; by Haemophilus IbpA; alternate => ECO:0000269|PubMed:19362538
source Swiss-Prot : SWS_FT_FI3

33) chain A
residue 35
type MOD_RES
sequence T
description (Microbial infection) O-AMP-threonine; by Vibrio VopS => ECO:0000269|PubMed:19039103
source Swiss-Prot : SWS_FT_FI4

34) chain A
residue 71
type MOD_RES
sequence S
description Phosphoserine => ECO:0000269|PubMed:10617634
source Swiss-Prot : SWS_FT_FI5

35) chain A
residue 32
type CARBOHYD
sequence Y
description (Microbial infection) O-linked (GlcNAc) tyrosine; by Photorhabdus PAU_02230; alternate => ECO:0000269|PubMed:24141704
source Swiss-Prot : SWS_FT_FI6

36) chain A
residue 35
type CARBOHYD
sequence T
description (Microbial infection) O-linked (Glc) threonine; by C.difficile toxins TcdA and TcdB, and by P.sordellii toxin TcsL; alternate => ECO:0000269|PubMed:19744486, ECO:0000269|PubMed:24905543, ECO:0000269|PubMed:7775453, ECO:0000269|PubMed:7777059
source Swiss-Prot : SWS_FT_FI7

37) chain A
residue 147
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:18093184
source Swiss-Prot : SWS_FT_FI8

38) chain A
residue 166
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:23512198
source Swiss-Prot : SWS_FT_FI9


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