eF-site ID 3sc1-A PDB Code 3sc1 Chain A click to enlarge Title Novel Isoquinolone PDK1 Inhibitors Discovered through Fragment-Based Lead Discovery Classification TRANSFERASE/TRANSFERASE INHIBITOR Compound 3-phosphoinositide-dependent protein kinase 1 Source Homo sapiens (Human) (PDPK1_HUMAN) Sequence A:  QPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKI LEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDD EKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSA LEYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSN XFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLP PFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLD ATKRLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLT Description (1)  3-phosphoinositide-dependent protein kinase 1 (E.C.2.7.11.1) Functional site 1) chain A residue 89 type sequence G description BINDING SITE FOR RESIDUE 3S1 A 900 source : AC1 2) chain A residue 90 type sequence E description BINDING SITE FOR RESIDUE 3S1 A 900 source : AC1 3) chain A residue 91 type sequence G description BINDING SITE FOR RESIDUE 3S1 A 900 source : AC1 4) chain A residue 109 type sequence A description BINDING SITE FOR RESIDUE 3S1 A 900 source : AC1 5) chain A residue 160 type sequence S description BINDING SITE FOR RESIDUE 3S1 A 900 source : AC1 6) chain A residue 161 type sequence Y description BINDING SITE FOR RESIDUE 3S1 A 900 source : AC1 7) chain A residue 162 type sequence A description BINDING SITE FOR RESIDUE 3S1 A 900 source : AC1 8) chain A residue 166 type sequence E description BINDING SITE FOR RESIDUE 3S1 A 900 source : AC1 9) chain A residue 212 type sequence L description BINDING SITE FOR RESIDUE 3S1 A 900 source : AC1 10) chain A residue 222 type sequence T description BINDING SITE FOR RESIDUE 3S1 A 900 source : AC1 11) chain A residue 106 type sequence R description BINDING SITE FOR RESIDUE SO4 A 901 source : AC2 12) chain A residue 140 type sequence P description BINDING SITE FOR RESIDUE SO4 A 901 source : AC2 13) chain A residue 351 type sequence H description BINDING SITE FOR RESIDUE SO4 A 901 source : AC2 14) chain A residue 76 type sequence K description BINDING SITE FOR RESIDUE SO4 A 902 source : AC3 15) chain A residue 131 type sequence R description BINDING SITE FOR RESIDUE SO4 A 902 source : AC3 16) chain A residue 148 type sequence T description BINDING SITE FOR RESIDUE SO4 A 902 source : AC3 17) chain A residue 149 type sequence F description BINDING SITE FOR RESIDUE SO4 A 902 source : AC3 18) chain A residue 150 type sequence Q description BINDING SITE FOR RESIDUE SO4 A 902 source : AC3 19) chain A residue 144 type sequence K description BINDING SITE FOR RESIDUE SO4 A 903 source : AC4 20) chain A residue 144 type sequence K description BINDING SITE FOR RESIDUE SO4 A 903 source : AC4 21) chain A residue 146 type sequence Y description BINDING SITE FOR RESIDUE SO4 A 903 source : AC4 22) chain A residue 146 type sequence Y description BINDING SITE FOR RESIDUE SO4 A 903 source : AC4 23) chain A residue 91 type sequence G description BINDING SITE FOR RESIDUE SO4 A 904 source : AC5 24) chain A residue 92 type sequence S description BINDING SITE FOR RESIDUE SO4 A 904 source : AC5 25) chain A residue 93 type sequence F description BINDING SITE FOR RESIDUE SO4 A 904 source : AC5 26) chain A residue 94 type sequence S description BINDING SITE FOR RESIDUE SO4 A 904 source : AC5 27) chain A residue 107 type sequence E description BINDING SITE FOR RESIDUE GOL A 905 source : AC6 28) chain A residue 146 type sequence Y description BINDING SITE FOR RESIDUE GOL A 905 source : AC6 29) chain A residue 160 type sequence S description BINDING SITE FOR RESIDUE GOL A 905 source : AC6 30) chain A residue 161 type sequence Y description BINDING SITE FOR RESIDUE GOL A 905 source : AC6 31) chain A residue 103 type sequence A description BINDING SITE FOR RESIDUE GOL A 906 source : AC7 32) chain A residue 104 type sequence T description BINDING SITE FOR RESIDUE GOL A 906 source : AC7 33) chain A residue 105 type sequence S description BINDING SITE FOR RESIDUE GOL A 906 source : AC7 34) chain A residue 139 type sequence H description BINDING SITE FOR RESIDUE GOL A 906 source : AC7 35) chain A residue 191 type sequence S description BINDING SITE FOR RESIDUE GOL A 906 source : AC7 36) chain A residue 347 type sequence W description BINDING SITE FOR RESIDUE GOL A 906 source : AC7 37) chain A residue 349 type sequence N description BINDING SITE FOR RESIDUE GOL A 906 source : AC7 38) chain A residue 350 type sequence L description BINDING SITE FOR RESIDUE GOL A 906 source : AC7 39) chain A residue 351 type sequence H description BINDING SITE FOR RESIDUE GOL A 906 source : AC7 40) chain A residue 304 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q9Z2A0 source Swiss-Prot : SWS_FT_FI5 41) chain A residue 354 type MOD_RES sequence T description Phosphothreonine; by MELK => ECO:0000269|PubMed:22544756 source Swiss-Prot : SWS_FT_FI6 42) chain A residue 92 type BINDING sequence S description BINDING => ECO:0000269|PubMed:12169624, ECO:0000269|PubMed:15741170, ECO:0000269|PubMed:22999883 source Swiss-Prot : SWS_FT_FI2 43) chain A residue 111 type BINDING sequence K description BINDING => ECO:0000269|PubMed:12169624, ECO:0000269|PubMed:15741170, ECO:0000269|PubMed:22999883 source Swiss-Prot : SWS_FT_FI2 44) chain A residue 160 type BINDING sequence S description BINDING => ECO:0000269|PubMed:12169624, ECO:0000269|PubMed:15741170, ECO:0000269|PubMed:22999883 source Swiss-Prot : SWS_FT_FI2 45) chain A residue 166 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12169624, ECO:0000269|PubMed:15741170, ECO:0000269|PubMed:22999883 source Swiss-Prot : SWS_FT_FI2 46) chain A residue 223 type BINDING sequence D description BINDING => ECO:0000269|PubMed:12169624, ECO:0000269|PubMed:15741170, ECO:0000269|PubMed:22999883 source Swiss-Prot : SWS_FT_FI2 47) chain A residue 209 type BINDING sequence E description BINDING => ECO:0000269|PubMed:22999883 source Swiss-Prot : SWS_FT_FI3 48) chain A residue 205 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 49) chain A residue 241 type MOD_RES sequence X description Phosphoserine; by autocatalysis => ECO:0000269|PubMed:10455013, ECO:0000269|PubMed:11481331, ECO:0000269|PubMed:15772071, ECO:0000269|PubMed:16780920, ECO:0000269|Ref.8 source Swiss-Prot : SWS_FT_FI4 50) chain A residue 88-111 type prosite sequence LGEGSFSTVVLARELATSREYAIK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGSFSTVVlArelatsre..........YAIK source prosite : PS00107 51) chain A residue 201-213 type prosite sequence IIHRDLKPENILL description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKpeNILL source prosite : PS00108

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