eF-site ID 5lvp-D PDB Code 5lvp Chain D 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 D:  PRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKIL EKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDE KLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSAL EYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLNXF VGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPF RAGNEGLIFAKIIKLEYDFPEKFFPKARDLVEKLLVLDAT KRLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLT Description (1)  3-phosphoinositide-dependent protein kinase 1 (E.C.2.7.11.1), hydrophobic-motif peptide of PKB/Akt Functional site 1) chain D residue 89 type sequence G description binding site for residue ATP D 500 source : AC5 2) chain D residue 90 type sequence E description binding site for residue ATP D 500 source : AC5 3) chain D residue 91 type sequence G description binding site for residue ATP D 500 source : AC5 4) chain D residue 92 type sequence S description binding site for residue ATP D 500 source : AC5 5) chain D residue 94 type sequence S description binding site for residue ATP D 500 source : AC5 6) chain D residue 96 type sequence V description binding site for residue ATP D 500 source : AC5 7) chain D residue 109 type sequence A description binding site for residue ATP D 500 source : AC5 8) chain D residue 111 type sequence K description binding site for residue ATP D 500 source : AC5 9) chain D residue 160 type sequence S description binding site for residue ATP D 500 source : AC5 10) chain D residue 162 type sequence A description binding site for residue ATP D 500 source : AC5 11) chain D residue 166 type sequence E description binding site for residue ATP D 500 source : AC5 12) chain D residue 212 type sequence L description binding site for residue ATP D 500 source : AC5 13) chain D residue 131 type sequence R description binding site for Di-peptide PHE H 11 and SEP H 12 source : AD3 14) chain D residue 148 type sequence T description binding site for Di-peptide PHE H 11 and SEP H 12 source : AD3 15) chain D residue 149 type sequence F description binding site for Di-peptide PHE H 11 and SEP H 12 source : AD3 16) chain D residue 150 type sequence Q description binding site for Di-peptide PHE H 11 and SEP H 12 source : AD3 17) chain D residue 155 type sequence L description binding site for Di-peptide PHE H 11 and SEP H 12 source : AD3 18) chain D residue 157 type sequence F description binding site for Di-peptide PHE H 11 and SEP H 12 source : AD3 19) chain D residue 135 type sequence S description binding site for Di-peptide SEP H 12 and TYR H 13 source : AD4 20) chain D residue 145 type sequence L description binding site for Di-peptide SEP H 12 and TYR H 13 source : AD4 21) chain D residue 148 type sequence T description binding site for Di-peptide SEP H 12 and TYR H 13 source : AD4 22) chain D residue 150 type sequence Q description binding site for Di-peptide SEP H 12 and TYR H 13 source : AD4 23) chain D 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 24) chain D 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 25) chain D 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 26) chain D 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 27) chain D 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 28) chain D 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 29) chain D residue 209 type BINDING sequence E description BINDING => ECO:0000269|PubMed:22999883 source Swiss-Prot : SWS_FT_FI3 30) chain D 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 31) chain D residue 304 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q9Z2A0 source Swiss-Prot : SWS_FT_FI5 32) chain D residue 354 type MOD_RES sequence T description Phosphothreonine; by MELK => ECO:0000269|PubMed:22544756 source Swiss-Prot : SWS_FT_FI6

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