eF-site ID 2xck-A PDB Code 2xck Chain A click to enlarge Title Crystal structure of PDK1 in complex with a pyrazoloquinazoline inhibitor Classification TRANSFERASE Compound 3-PHOSPHOINOSITIDE DEPENDENT PROTEIN KINASE 1 Source Homo sapiens (Human) (PDPK1_HUMAN) Sequence A:  KKRPEDFKFGKILGEGSFSTTVLARELATSREYAIKILEK RHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKL YFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEY LHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSNXFV GTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFR AGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATK RLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLT Description Functional site 1) chain A residue 103 type sequence A description BINDING SITE FOR RESIDUE GOL A 1361 source : AC1 2) chain A residue 104 type sequence T description BINDING SITE FOR RESIDUE GOL A 1361 source : AC1 3) chain A residue 139 type sequence H description BINDING SITE FOR RESIDUE GOL A 1361 source : AC1 4) chain A residue 191 type sequence S description BINDING SITE FOR RESIDUE GOL A 1361 source : AC1 5) chain A residue 347 type sequence W description BINDING SITE FOR RESIDUE GOL A 1361 source : AC1 6) chain A residue 348 type sequence E description BINDING SITE FOR RESIDUE GOL A 1361 source : AC1 7) chain A residue 349 type sequence N description BINDING SITE FOR RESIDUE GOL A 1361 source : AC1 8) chain A residue 350 type sequence L description BINDING SITE FOR RESIDUE GOL A 1361 source : AC1 9) chain A residue 351 type sequence H description BINDING SITE FOR RESIDUE GOL A 1361 source : AC1 10) chain A residue 82 type sequence F description BINDING SITE FOR RESIDUE GOL A 1362 source : AC2 11) chain A residue 83 type sequence K description BINDING SITE FOR RESIDUE GOL A 1362 source : AC2 12) chain A residue 84 type sequence F description BINDING SITE FOR RESIDUE GOL A 1362 source : AC2 13) chain A residue 194 type sequence E description BINDING SITE FOR RESIDUE GOL A 1362 source : AC2 14) chain A residue 334 type sequence G description BINDING SITE FOR RESIDUE GOL A 1362 source : AC2 15) chain A residue 337 type sequence K description BINDING SITE FOR RESIDUE GOL A 1362 source : AC2 16) chain A residue 106 type sequence R description BINDING SITE FOR RESIDUE GOL A 1363 source : AC3 17) chain A residue 107 type sequence E description BINDING SITE FOR RESIDUE GOL A 1363 source : AC3 18) chain A residue 146 type sequence Y description BINDING SITE FOR RESIDUE GOL A 1363 source : AC3 19) chain A residue 160 type sequence S description BINDING SITE FOR RESIDUE GOL A 1363 source : AC3 20) chain A residue 161 type sequence Y description BINDING SITE FOR RESIDUE GOL A 1363 source : AC3 21) chain A residue 106 type sequence R description BINDING SITE FOR RESIDUE GOL A 1365 source : AC4 22) chain A residue 107 type sequence E description BINDING SITE FOR RESIDUE GOL A 1365 source : AC4 23) chain A residue 351 type sequence H description BINDING SITE FOR RESIDUE GOL A 1365 source : AC4 24) chain A residue 352 type sequence Q description BINDING SITE FOR RESIDUE GOL A 1365 source : AC4 25) chain A residue 76 type sequence K description BINDING SITE FOR RESIDUE SO4 A 1368 source : AC5 26) chain A residue 131 type sequence R description BINDING SITE FOR RESIDUE SO4 A 1368 source : AC5 27) chain A residue 148 type sequence T description BINDING SITE FOR RESIDUE SO4 A 1368 source : AC5 28) chain A residue 149 type sequence F description BINDING SITE FOR RESIDUE SO4 A 1368 source : AC5 29) chain A residue 150 type sequence Q description BINDING SITE FOR RESIDUE SO4 A 1368 source : AC5 30) chain A residue 144 type sequence K description BINDING SITE FOR RESIDUE SO4 A 1369 source : AC6 31) chain A residue 144 type sequence K description BINDING SITE FOR RESIDUE SO4 A 1369 source : AC6 32) chain A residue 146 type sequence Y description BINDING SITE FOR RESIDUE SO4 A 1369 source : AC6 33) chain A residue 146 type sequence Y description BINDING SITE FOR RESIDUE SO4 A 1369 source : AC6 34) chain A residue 106 type sequence R description BINDING SITE FOR RESIDUE SO4 A 1370 source : AC7 35) chain A residue 351 type sequence H description BINDING SITE FOR RESIDUE SO4 A 1370 source : AC7 36) chain A residue 88 type sequence L description BINDING SITE FOR RESIDUE MH4 A 1360 source : AC8 37) chain A residue 91 type sequence G description BINDING SITE FOR RESIDUE MH4 A 1360 source : AC8 38) chain A residue 94 type sequence S description BINDING SITE FOR RESIDUE MH4 A 1360 source : AC8 39) chain A residue 109 type sequence A description BINDING SITE FOR RESIDUE MH4 A 1360 source : AC8 40) chain A residue 111 type sequence K description BINDING SITE FOR RESIDUE MH4 A 1360 source : AC8 41) chain A residue 159 type sequence L description BINDING SITE FOR RESIDUE MH4 A 1360 source : AC8 42) chain A residue 160 type sequence S description BINDING SITE FOR RESIDUE MH4 A 1360 source : AC8 43) chain A residue 162 type sequence A description BINDING SITE FOR RESIDUE MH4 A 1360 source : AC8 44) chain A residue 212 type sequence L description BINDING SITE FOR RESIDUE MH4 A 1360 source : AC8 45) chain A residue 222 type sequence T description BINDING SITE FOR RESIDUE MH4 A 1360 source : AC8 46) chain A residue 223 type sequence D description BINDING SITE FOR RESIDUE MH4 A 1360 source : AC8 47) chain A residue 255 type ACT_SITE sequence T description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 48) chain A residue 142 type BINDING sequence F description BINDING => ECO:0000269|PubMed:12169624, ECO:0000269|PubMed:15741170, ECO:0000269|PubMed:22999883 source Swiss-Prot : SWS_FT_FI2 49) chain A residue 161 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:12169624, ECO:0000269|PubMed:15741170, ECO:0000269|PubMed:22999883 source Swiss-Prot : SWS_FT_FI2 50) chain A residue 210 type BINDING sequence N description BINDING => ECO:0000269|PubMed:12169624, ECO:0000269|PubMed:15741170, ECO:0000269|PubMed:22999883 source Swiss-Prot : SWS_FT_FI2 51) chain A residue 216 type BINDING sequence D description BINDING => ECO:0000269|PubMed:12169624, ECO:0000269|PubMed:15741170, ECO:0000269|PubMed:22999883 source Swiss-Prot : SWS_FT_FI2 52) chain A residue 273 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:12169624, ECO:0000269|PubMed:15741170, ECO:0000269|PubMed:22999883 source Swiss-Prot : SWS_FT_FI2 53) chain A residue 259 type BINDING sequence A description BINDING => ECO:0000269|PubMed:22999883 source Swiss-Prot : SWS_FT_FI3 54) chain A residue 291 type MOD_RES sequence F 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_FI6 55) chain A residue 88-111 type prosite sequence LGEGSFSTTVLARELATSREYAIK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGSFSTTVlArelatsre..........YAIK source prosite : PS00107 56) chain A residue 201-213 type prosite sequence IIHRDLKPENILL description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKpeNILL source prosite : PS00108 57) chain A residue 354 type MOD_RES sequence T description N6-acetyllysine => ECO:0000250|UniProtKB:Q9Z2A0 source Swiss-Prot : SWS_FT_FI7

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