eF-site ID 5lvp-A PDB Code 5lvp Chain A click to enlarge Title Human PDK1 Kinase Domain in Complex with an HM-Peptide Bound to the PIF-Pocket Classification TRANSFERASE Compound 3-phosphoinositide-dependent protein kinase 1 Source (5LVP) Sequence A:  RKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILE KRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEK LYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALE YLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLNXFV GTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFR AGNEGLIFAKIIKLEYDFPEKFFPKARDLVEKLLVLDATK RLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLT Description (1)  3-phosphoinositide-dependent protein kinase 1 (E.C.2.7.11.1), hydrophobic-motif peptide of PKB/Akt Functional site 1) chain A residue 89 type sequence G description binding site for residue ATP A 500 source : AC1 2) chain A residue 91 type sequence G description binding site for residue ATP A 500 source : AC1 3) chain A residue 92 type sequence S description binding site for residue ATP A 500 source : AC1 4) chain A residue 94 type sequence S description binding site for residue ATP A 500 source : AC1 5) chain A residue 96 type sequence V description binding site for residue ATP A 500 source : AC1 6) chain A residue 109 type sequence A description binding site for residue ATP A 500 source : AC1 7) chain A residue 111 type sequence K description binding site for residue ATP A 500 source : AC1 8) chain A residue 160 type sequence S description binding site for residue ATP A 500 source : AC1 9) chain A residue 162 type sequence A description binding site for residue ATP A 500 source : AC1 10) chain A residue 166 type sequence E description binding site for residue ATP A 500 source : AC1 11) chain A residue 212 type sequence L description binding site for residue ATP A 500 source : AC1 12) chain A residue 131 type sequence R description binding site for Di-peptide PHE F 11 and SEP F 12 source : AC8 13) chain A residue 148 type sequence T description binding site for Di-peptide PHE F 11 and SEP F 12 source : AC8 14) chain A residue 149 type sequence F description binding site for Di-peptide PHE F 11 and SEP F 12 source : AC8 15) chain A residue 150 type sequence Q description binding site for Di-peptide PHE F 11 and SEP F 12 source : AC8 16) chain A residue 157 type sequence F description binding site for Di-peptide PHE F 11 and SEP F 12 source : AC8 17) chain A residue 135 type sequence S description binding site for Di-peptide SEP F 12 and TYR F 13 source : AC9 18) chain A residue 147 type sequence F description binding site for Di-peptide SEP F 12 and TYR F 13 source : AC9 19) chain A residue 148 type sequence T description binding site for Di-peptide SEP F 12 and TYR F 13 source : AC9 20) chain A residue 150 type sequence Q description binding site for Di-peptide SEP F 12 and TYR F 13 source : AC9 21) 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 22) 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 23) 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 24) 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 25) 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 26) 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 27) chain A residue 209 type BINDING sequence E description BINDING => ECO:0000269|PubMed:22999883 source Swiss-Prot : SWS_FT_FI3 28) 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 29) chain A residue 304 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q9Z2A0 source Swiss-Prot : SWS_FT_FI5 30) chain A residue 354 type MOD_RES sequence T description Phosphothreonine; by MELK => ECO:0000269|PubMed:22544756 source Swiss-Prot : SWS_FT_FI6 31) chain A residue 88-111 type prosite sequence LGEGSFSTVVLARELATSREYAIK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGSFSTVVlArelatsre..........YAIK source prosite : PS00107 32) 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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