eF-site ID 4a4l-A PDB Code 4a4l Chain A click to enlarge Title CRYSTAL STRUCTURE OF POLO-LIKE KINASE 1 IN COMPLEX WITH A 5-(2-AMINO- PYRIMIDIN-4-YL)-1H-PYRROLE INHIBITOR Classification TRANSFERASE Compound SERINE/THREONINE-PROTEIN KINASE PLK1 Source (PLK1_HUMAN) Sequence A:  EIPEVLVDPRSRRRYVRGRFLGKGGFAKCFEISDADTKEV FAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHG FFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLR QIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLA TKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIG CIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVA ASLIQKMLQTDPTARPTINELLNDEFFTSGYIPARLPITC LTIPPRFSIAP Description (1)  SERINE/THREONINE-PROTEIN KINASE PLK1 (E.C.2.7.11.21) Functional site 1) chain A residue 93 type sequence H description BINDING SITE FOR RESIDUE ZN A 1329 source : AC1 2) chain A residue 212 type sequence C description BINDING SITE FOR RESIDUE ZN A 1329 source : AC1 3) chain A residue 255 type sequence C description BINDING SITE FOR RESIDUE ZN A 1329 source : AC1 4) chain A residue 91 type sequence K description BINDING SITE FOR RESIDUE TLA A 1330 source : AC2 5) chain A residue 93 type sequence H description BINDING SITE FOR RESIDUE TLA A 1330 source : AC2 6) chain A residue 94 type sequence Q description BINDING SITE FOR RESIDUE TLA A 1330 source : AC2 7) chain A residue 97 type sequence K description BINDING SITE FOR RESIDUE TLA A 1330 source : AC2 8) chain A residue 212 type sequence C description BINDING SITE FOR RESIDUE TLA A 1330 source : AC2 9) chain A residue 255 type sequence C description BINDING SITE FOR RESIDUE TLA A 1330 source : AC2 10) chain A residue 256 type sequence L description BINDING SITE FOR RESIDUE TLA A 1330 source : AC2 11) chain A residue 57 type sequence R description BINDING SITE FOR RESIDUE 939 A 1331 source : AC3 12) chain A residue 59 type sequence L description BINDING SITE FOR RESIDUE 939 A 1331 source : AC3 13) chain A residue 67 type sequence C description BINDING SITE FOR RESIDUE 939 A 1331 source : AC3 14) chain A residue 80 type sequence A description BINDING SITE FOR RESIDUE 939 A 1331 source : AC3 15) chain A residue 82 type sequence K description BINDING SITE FOR RESIDUE 939 A 1331 source : AC3 16) chain A residue 131 type sequence E description BINDING SITE FOR RESIDUE 939 A 1331 source : AC3 17) chain A residue 132 type sequence L description BINDING SITE FOR RESIDUE 939 A 1331 source : AC3 18) chain A residue 133 type sequence C description BINDING SITE FOR RESIDUE 939 A 1331 source : AC3 19) chain A residue 134 type sequence R description BINDING SITE FOR RESIDUE 939 A 1331 source : AC3 20) chain A residue 136 type sequence R description BINDING SITE FOR RESIDUE 939 A 1331 source : AC3 21) chain A residue 137 type sequence S description BINDING SITE FOR RESIDUE 939 A 1331 source : AC3 22) chain A residue 140 type sequence E description BINDING SITE FOR RESIDUE 939 A 1331 source : AC3 23) chain A residue 180 type sequence G description BINDING SITE FOR RESIDUE 939 A 1331 source : AC3 24) chain A residue 183 type sequence F description BINDING SITE FOR RESIDUE 939 A 1331 source : AC3 25) chain A residue 194 type sequence D description BINDING SITE FOR RESIDUE 939 A 1331 source : AC3 26) chain A residue 269 type MOD_RES sequence S description Phosphoserine; by autocatalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI7 27) chain A residue 210 type MOD_RES sequence T description Phosphothreonine; by AURKA => ECO:0000269|PubMed:12207013, ECO:0000269|PubMed:18477460, ECO:0000269|PubMed:18615013, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 28) chain A residue 59-82 type prosite sequence LGKGGFAKCFEISDADTKEVFAGK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGGFAKCFeIsdadtkev..........FAGK source prosite : PS00107 29) chain A residue 172-184 type prosite sequence VIHRDLKLGNLFL description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDLKlgNLFL source prosite : PS00108 30) chain A residue 176 type ACT_SITE sequence D description Proton acceptor => ECO:0000269|PubMed:18615013 source Swiss-Prot : SWS_FT_FI1 31) chain A residue 59 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 32) chain A residue 82 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 33) chain A residue 131 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 34) chain A residue 178 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 35) chain A residue 194 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 36) chain A residue 103 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18691976 source Swiss-Prot : SWS_FT_FI3 37) chain A residue 137 type MOD_RES sequence S description Phosphoserine => ECO:0000305|PubMed:12207013 source Swiss-Prot : SWS_FT_FI4 38) chain A residue 214 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI6

Display surface Download Links