eF-site ID 5euq-BE PDB Code 5euq Chain B, E click to enlarge Title Crystal structure of an engineered construct of phosphatidylinositol 4 kinase III beta with a potent and selective inhibitor in complex with GDP loaded Rab11 Classification Transferase/Signaling Protein Compound Ras-related protein Rab-11A Source (PI4KB_HUMAN) Sequence B:  EYDYLFKVVLIGDSGVGKSNLLSRFTRNEFNLESGVEFAT RSIQVDGKTIKAQIWDTATSAYYRGAVGALLVYDIAKHLT YENVERWLKELRDHADSNIVIMLVGNKSDLRHLRAVPTDE ARAFAEKNGLSFIETSALDSTNVEAAFQTILTEIY E:  SWLLRLFESKLFDISMAISYLYNSKEPGVQAYIGNRLFCF RNEDVDFYLPQLLNMYIHMDEDVGDAIKPYIVHRCRQSIN FSLQCALLLGAYSSRGTKLRKLILSRLAPEREFIKSLMAI GKRLATLPTKEQKTQRLISELSLLNHKLPARVWLPTAGFD HHVVRVPHTQAVVLNSKDKAPYLIYVEVLECENFDTTSVP ARIPPSAVALKEPWQEKVRRIREGSPYGHLPNWRLLSVIV KCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVI SADSGMIEPVVNAVSIHQVKKQSQLSLLDYFLQEHGSYTT EAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEG HIIHIDFGFILSSSPKLTTEFVDVMGGLDGDMFNYYKMLM LQGLIAARKHMDKVVQIVEIMQQGSQLPCFHGSSTIRNLK ERFHMSMTEEQLQLLVEQMVDGSM Description Functional site 1) chain B residue 20 type sequence S description binding site for residue GDP B 301 source : AC1 2) chain B residue 21 type sequence G description binding site for residue GDP B 301 source : AC1 3) chain B residue 22 type sequence V description binding site for residue GDP B 301 source : AC1 4) chain B residue 23 type sequence G description binding site for residue GDP B 301 source : AC1 5) chain B residue 24 type sequence K description binding site for residue GDP B 301 source : AC1 6) chain B residue 25 type sequence S description binding site for residue GDP B 301 source : AC1 7) chain B residue 26 type sequence N description binding site for residue GDP B 301 source : AC1 8) chain B residue 36 type sequence F description binding site for residue GDP B 301 source : AC1 9) chain B residue 37 type sequence N description binding site for residue GDP B 301 source : AC1 10) chain B residue 38 type sequence L description binding site for residue GDP B 301 source : AC1 11) chain B residue 124 type sequence N description binding site for residue GDP B 301 source : AC1 12) chain B residue 125 type sequence K description binding site for residue GDP B 301 source : AC1 13) chain B residue 127 type sequence D description binding site for residue GDP B 301 source : AC1 14) chain B residue 128 type sequence L description binding site for residue GDP B 301 source : AC1 15) chain B residue 154 type sequence S description binding site for residue GDP B 301 source : AC1 16) chain B residue 155 type sequence A description binding site for residue GDP B 301 source : AC1 17) chain B residue 156 type sequence L description binding site for residue GDP B 301 source : AC1 18) chain E residue 605 type sequence H description binding site for residue SO4 E 1001 source : AC2 19) chain E residue 608 type sequence K description binding site for residue SO4 E 1001 source : AC2 20) chain E residue 659 type sequence N description binding site for residue SO4 E 1001 source : AC2 21) chain E residue 183 type sequence Y description binding site for residue SO4 E 1002 source : AC3 22) chain E residue 195 type sequence K description binding site for residue SO4 E 1002 source : AC3 23) chain E residue 232 type sequence R description binding site for residue SO4 E 1002 source : AC3 24) chain E residue 233 type sequence G description binding site for residue SO4 E 1002 source : AC3 25) chain E residue 235 type sequence K description binding site for residue SO4 E 1002 source : AC3 26) chain E residue 236 type sequence L description binding site for residue SO4 E 1002 source : AC3 27) chain E residue 374 type sequence L description binding site for residue 5S8 E 1003 source : AC4 28) chain E residue 381 type sequence P description binding site for residue 5S8 E 1003 source : AC4 29) chain E residue 547 type sequence I description binding site for residue 5S8 E 1003 source : AC4 30) chain E residue 549 type sequence K description binding site for residue 5S8 E 1003 source : AC4 31) chain E residue 583 type sequence Y description binding site for residue 5S8 E 1003 source : AC4 32) chain E residue 595 type sequence I description binding site for residue 5S8 E 1003 source : AC4 33) chain E residue 597 type sequence P description binding site for residue 5S8 E 1003 source : AC4 34) chain E residue 598 type sequence V description binding site for residue 5S8 E 1003 source : AC4 35) chain E residue 601 type sequence A description binding site for residue 5S8 E 1003 source : AC4 36) chain E residue 660 type sequence G description binding site for residue 5S8 E 1003 source : AC4 37) chain E residue 661 type sequence N description binding site for residue 5S8 E 1003 source : AC4 38) chain E residue 663 type sequence L description binding site for residue 5S8 E 1003 source : AC4 39) chain E residue 673 type sequence I description binding site for residue 5S8 E 1003 source : AC4 40) chain E residue 650 type MOD_RES sequence Y description Phosphoserine => ECO:0000269|PubMed:11277933, ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI8 41) chain E residue 656 type MOD_RES sequence D description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI9 42) chain B residue 14-27 type prosite sequence VVLIGDSGVGKSNL description SIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. VVLiGDSGVGKsnL source prosite : PS00675 43) chain E residue 548-562 type prosite sequence VKCGDDLRQELLAFQ description PI3_4_KINASE_1 Phosphatidylinositol 3- and 4-kinases signature 1. VKcg.DDLRQEllafQ source prosite : PS00915 44) chain E residue 641-661 type prosite sequence SCAGYCLVCYLLQVKDRHNGN description PI3_4_KINASE_2 Phosphatidylinositol 3- and 4-kinases signature 2. ScAgycLvcYLLqVkDRHngN source prosite : PS00916 45) chain B residue 124 type MOD_RES sequence N description Phosphoserine => ECO:0000269|PubMed:11277933, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 46) chain B residue 154 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:11277933, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 47) chain E residue 658 type MOD_RES sequence H description Phosphothreonine => ECO:0000269|PubMed:11277933 source Swiss-Prot : SWS_FT_FI2 48) chain E residue 577 type MOD_RES sequence P description Phosphothreonine => ECO:0000269|PubMed:11277933 source Swiss-Prot : SWS_FT_FI2 49) chain E residue 323 type MOD_RES sequence R description Phosphoserine => ECO:0000250|UniProtKB:Q8BKC8 source Swiss-Prot : SWS_FT_FI4 50) chain E residue 314 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:Q8BKC8 source Swiss-Prot : SWS_FT_FI4 51) chain E residue 316 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:11277933, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 52) chain E residue 333 type MOD_RES sequence K description Phosphoserine => ECO:0000269|PubMed:11277933, ECO:0000269|PubMed:23572552 source Swiss-Prot : SWS_FT_FI6 53) chain E residue 567 type MOD_RES sequence L description Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI7

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