eF-site ID 3q5i-A PDB Code 3q5i Chain A click to enlarge Title Crystal Structure of PBANKA_031420 Classification TRANSFERASE Compound Protein kinase Source (Q4YRR5_PLABE) Sequence A:  GRENLYFQGIAINPGMYVRKKEGKIGESYFKVRKLGSYGE VLLCKEKNGHSEKAIKVIKKKFHEEIYNEISLLKSLDHPN IIKLFDVFEDKKYFYLVTEFYEGGELFEQIINRHKFDECD AANIMKQILSGICYLHKHNIVHRDIKPENILLENKNSLLN IKIVDFGLSSFFSKDYKLRDRLGTAYYIAPEVLKKKYNEK CDVWSCGVIMYILLCGYPPFGGQNDQDIIKKVEKGKYYFD FNDWKNISDEAKELIKLMLTYDYNKRCTAEEALNSRWIKK YANNINKSDQKTLCGALSNMRKFEGSQKLAQAAILFIGSK LTTLEERKELTDIFKKLDKNGDGQLDKKELIEGYNVLRNF KLGELKNVEEEVDNILKEVDFDKNGYIEYSEFISVCMDKQ ILFSEERLRRAFNLFDTDKSGKITKEELANLFGLTSISEK TWNDVLGEADQNKDNMIDFDEFVSMMHKIC Description Functional site 1) chain A residue 384 type sequence D description BINDING SITE FOR RESIDUE CA A 1 source : AC1 2) chain A residue 386 type sequence N description BINDING SITE FOR RESIDUE CA A 1 source : AC1 3) chain A residue 388 type sequence D description BINDING SITE FOR RESIDUE CA A 1 source : AC1 4) chain A residue 390 type sequence Q description BINDING SITE FOR RESIDUE CA A 1 source : AC1 5) chain A residue 395 type sequence E description BINDING SITE FOR RESIDUE CA A 1 source : AC1 6) chain A residue 428 type sequence D description BINDING SITE FOR RESIDUE CA A 524 source : AC2 7) chain A residue 430 type sequence D description BINDING SITE FOR RESIDUE CA A 524 source : AC2 8) chain A residue 432 type sequence N description BINDING SITE FOR RESIDUE CA A 524 source : AC2 9) chain A residue 434 type sequence Y description BINDING SITE FOR RESIDUE CA A 524 source : AC2 10) chain A residue 436 type sequence E description BINDING SITE FOR RESIDUE CA A 524 source : AC2 11) chain A residue 439 type sequence E description BINDING SITE FOR RESIDUE CA A 524 source : AC2 12) chain A residue 464 type sequence D description BINDING SITE FOR RESIDUE CA A 525 source : AC3 13) chain A residue 466 type sequence D description BINDING SITE FOR RESIDUE CA A 525 source : AC3 14) chain A residue 468 type sequence S description BINDING SITE FOR RESIDUE CA A 525 source : AC3 15) chain A residue 470 type sequence K description BINDING SITE FOR RESIDUE CA A 525 source : AC3 16) chain A residue 475 type sequence E description BINDING SITE FOR RESIDUE CA A 525 source : AC3 17) chain A residue 498 type sequence D description BINDING SITE FOR RESIDUE CA A 526 source : AC4 18) chain A residue 500 type sequence N description BINDING SITE FOR RESIDUE CA A 526 source : AC4 19) chain A residue 502 type sequence D description BINDING SITE FOR RESIDUE CA A 526 source : AC4 20) chain A residue 504 type sequence M description BINDING SITE FOR RESIDUE CA A 526 source : AC4 21) chain A residue 509 type sequence E description BINDING SITE FOR RESIDUE CA A 526 source : AC4 22) chain A residue 195 type sequence N description BINDING SITE FOR RESIDUE CA A 528 source : AC5 23) chain A residue 211 type sequence D description BINDING SITE FOR RESIDUE CA A 528 source : AC5 24) chain A residue 71 type sequence V description BINDING SITE FOR RESIDUE ANP A 1634 source : AC6 25) chain A residue 84 type sequence A description BINDING SITE FOR RESIDUE ANP A 1634 source : AC6 26) chain A residue 86 type sequence K description BINDING SITE FOR RESIDUE ANP A 1634 source : AC6 27) chain A residue 128 type sequence I description BINDING SITE FOR RESIDUE ANP A 1634 source : AC6 28) chain A residue 144 type sequence T description BINDING SITE FOR RESIDUE ANP A 1634 source : AC6 29) chain A residue 145 type sequence E description BINDING SITE FOR RESIDUE ANP A 1634 source : AC6 30) chain A residue 146 type sequence F description BINDING SITE FOR RESIDUE ANP A 1634 source : AC6 31) chain A residue 147 type sequence Y description BINDING SITE FOR RESIDUE ANP A 1634 source : AC6 32) chain A residue 151 type sequence E description BINDING SITE FOR RESIDUE ANP A 1634 source : AC6 33) chain A residue 195 type sequence N description BINDING SITE FOR RESIDUE ANP A 1634 source : AC6 34) chain A residue 197 type sequence L description BINDING SITE FOR RESIDUE ANP A 1634 source : AC6 35) chain A residue 211 type sequence D description BINDING SITE FOR RESIDUE ANP A 1634 source : AC6 36) chain A residue 211 type sequence D description BINDING SITE FOR RESIDUE MG A 529 source : AC7 37) chain A residue 412 type sequence E description BINDING SITE FOR RESIDUE MG A 529 source : AC7 38) chain A residue 31 type sequence E description BINDING SITE FOR RESIDUE CA A 527 source : AC8 39) chain A residue 34 type sequence Y description BINDING SITE FOR RESIDUE CA A 527 source : AC8 40) chain A residue 35 type sequence F description BINDING SITE FOR RESIDUE CA A 527 source : AC8 41) chain A residue 36 type sequence Q description BINDING SITE FOR RESIDUE CA A 527 source : AC8 42) chain A residue 384-396 type prosite sequence DKNGDGQLDKKEL description EF_HAND_1 EF-hand calcium-binding domain. DKNGDGQLDkkEL source prosite : PS00018 43) chain A residue 428-440 type prosite sequence DFDKNGYIEYSEF description EF_HAND_1 EF-hand calcium-binding domain. DKNGDGQLDkkEL source prosite : PS00018 44) chain A residue 464-476 type prosite sequence DTDKSGKITKEEL description EF_HAND_1 EF-hand calcium-binding domain. DKNGDGQLDkkEL source prosite : PS00018 45) chain A residue 498-510 type prosite sequence DQNKDNMIDFDEF description EF_HAND_1 EF-hand calcium-binding domain. DKNGDGQLDkkEL source prosite : PS00018 46) chain A residue 63-90 type prosite sequence LGSYGEVLLCKEKNGHSEKAIKVIKK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGAYGEVLlCkeknghsekaik......VIKK source prosite : PS00107 47) chain A residue 186-198 type prosite sequence IVHRDIKPENILL description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDIKpeNILL source prosite : PS00108 48) chain A residue 190 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 49) chain A residue 63 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 50) chain A residue 86 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 51) chain A residue 90 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU10141 source Swiss-Prot : SWS_FT_FI3 52) chain A residue 384 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI4 53) chain A residue 386 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI4 54) chain A residue 388 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI4 55) chain A residue 390 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI4 56) chain A residue 395 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI4 57) chain A residue 428 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI4 58) chain A residue 430 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI4 59) chain A residue 432 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI4 60) chain A residue 434 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI4 61) chain A residue 439 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI4 62) chain A residue 464 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI4 63) chain A residue 466 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI4 64) chain A residue 468 type BINDING sequence S description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI4 65) chain A residue 470 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI4 66) chain A residue 475 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI4 67) chain A residue 498 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI4 68) chain A residue 500 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI4 69) chain A residue 502 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI4 70) chain A residue 504 type BINDING sequence M description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI4 71) chain A residue 509 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI4 72) chain A residue 65 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P62344 source Swiss-Prot : SWS_FT_FI5 73) chain A residue 117 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P62344 source Swiss-Prot : SWS_FT_FI5 74) chain A residue 216 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P62344 source Swiss-Prot : SWS_FT_FI5 75) chain A residue 219 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P62344 source Swiss-Prot : SWS_FT_FI5 76) chain A residue 334 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P62344 source Swiss-Prot : SWS_FT_FI5 77) chain A residue 230 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P62344 source Swiss-Prot : SWS_FT_FI6

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