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