eF-site ID 2buj-AB PDB Code 2buj Chain A, B click to enlarge Title Crystal structure of the human Serine-threonine Kinase 16 in complex with staurosporine Classification TRANSFERASE Compound SERINE/THREONINE-PROTEIN KINASE 16 Source (STK16_HUMAN) Sequence A:  NLYFQGHMVIIDNKHYLFIQKLGEFSYVDLVEGLHDGHFY ALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLR ERGAKHEAWLLLPFFKRGTLWNEIERLKDKGNFLTEDQIL WLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMD LGSMNQACIHVEGSRQALTLQDWAAQRCTISYRAPELFSV QSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVA LAVQNQIPQSPRHSSALWQLLNSMMTVDPHQRPHIPLLLS QLEALQPPAPG B:  ENLYFQGHMVIIDNKHYLFIQKLGEGGFSYVDLVEGLHDG HFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAY CLREHEAWLLLPFFKRGTLWNEIERLKDKGNFLTEDQILW LLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDL GSMNQACIHVEGSRQALTLQDWAAQRCTISYRAPELFSVQ SHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVAL AVQNQLSPRHSSALWQLLNSMMTVDPHQRPHIPLLLSQLE ALQPPA Description (1)  SERINE/THREONINE-PROTEIN KINASE 16 (E.C.2.7.1.37) Functional site 1) chain A residue 59 type sequence R description BINDING SITE FOR RESIDUE CL A1300 source : AC1 2) chain B residue 30 type sequence G description BINDING SITE FOR RESIDUE CL B1298 source : AC2 3) chain B residue 32 type sequence S description BINDING SITE FOR RESIDUE CL B1298 source : AC2 4) chain A residue 26 type sequence L description BINDING SITE FOR RESIDUE STU A1301 source : AC3 5) chain A residue 28 type sequence E description BINDING SITE FOR RESIDUE STU A1301 source : AC3 6) chain A residue 34 type sequence V description BINDING SITE FOR RESIDUE STU A1301 source : AC3 7) chain A residue 47 type sequence A description BINDING SITE FOR RESIDUE STU A1301 source : AC3 8) chain A residue 99 type sequence P description BINDING SITE FOR RESIDUE STU A1301 source : AC3 9) chain A residue 100 type sequence F description BINDING SITE FOR RESIDUE STU A1301 source : AC3 10) chain A residue 101 type sequence F description BINDING SITE FOR RESIDUE STU A1301 source : AC3 11) chain A residue 165 type sequence M description BINDING SITE FOR RESIDUE STU A1301 source : AC3 12) chain A residue 87 type sequence E description BINDING SITE FOR RESIDUE STU A1302 source : AC4 13) chain A residue 92 type sequence H description BINDING SITE FOR RESIDUE STU A1302 source : AC4 14) chain B residue 24 type sequence Q description BINDING SITE FOR RESIDUE STU A1302 source : AC4 15) chain B residue 26 type sequence L description BINDING SITE FOR RESIDUE STU B1299 source : AC5 16) chain B residue 27 type sequence G description BINDING SITE FOR RESIDUE STU B1299 source : AC5 17) chain B residue 28 type sequence E description BINDING SITE FOR RESIDUE STU B1299 source : AC5 18) chain B residue 47 type sequence A description BINDING SITE FOR RESIDUE STU B1299 source : AC5 19) chain B residue 99 type sequence P description BINDING SITE FOR RESIDUE STU B1299 source : AC5 20) chain B residue 100 type sequence F description BINDING SITE FOR RESIDUE STU B1299 source : AC5 21) chain B residue 101 type sequence F description BINDING SITE FOR RESIDUE STU B1299 source : AC5 22) chain B residue 165 type sequence M description BINDING SITE FOR RESIDUE STU B1299 source : AC5 23) chain A residue 54 type sequence H description BINDING SITE FOR RESIDUE STU B1300 source : AC6 24) chain A residue 55 type sequence E description BINDING SITE FOR RESIDUE STU B1300 source : AC6 25) chain B residue 24 type sequence Q description BINDING SITE FOR RESIDUE STU B1300 source : AC6 26) chain B residue 26 type sequence L description BINDING SITE FOR RESIDUE STU B1300 source : AC6 27) chain B residue 45 type sequence F description BINDING SITE FOR RESIDUE STU B1300 source : AC6 28) chain B residue 100 type sequence F description BINDING SITE FOR RESIDUE STU B1300 source : AC6 29) chain B residue 102 type sequence K description BINDING SITE FOR RESIDUE STU B1300 source : AC6 30) chain B residue 103 type sequence R description BINDING SITE FOR RESIDUE STU B1300 source : AC6 31) chain B residue 104 type sequence G description BINDING SITE FOR RESIDUE STU B1300 source : AC6 32) chain A residue 199 type MOD_RES sequence R description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:18184589 source Swiss-Prot : SWS_FT_FI5 33) chain B residue 199 type MOD_RES sequence R description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:18184589 source Swiss-Prot : SWS_FT_FI5 34) chain A residue 144-156 type prosite sequence YAHRDLKPTNILL description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. YaHrDLKptNILL source prosite : PS00108 35) chain A residue 149 type ACT_SITE sequence L description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 36) chain B residue 149 type ACT_SITE sequence L description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 37) chain A residue 27 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 38) chain A residue 50 type BINDING sequence R description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 39) chain B residue 27 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 40) chain B residue 50 type BINDING sequence R description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 41) chain A residue 186 type MOD_RES sequence L description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:18184589 source Swiss-Prot : SWS_FT_FI3 42) chain B residue 186 type MOD_RES sequence L description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:18184589 source Swiss-Prot : SWS_FT_FI3 43) chain A residue 198 type MOD_RES sequence Y description Phosphoserine; by autocatalysis => ECO:0000269|PubMed:18184589 source Swiss-Prot : SWS_FT_FI4 44) chain B residue 198 type MOD_RES sequence Y description Phosphoserine; by autocatalysis => ECO:0000269|PubMed:18184589 source Swiss-Prot : SWS_FT_FI4

Display surface Download Links