eF-site ID 5lvp-C PDB Code 5lvp Chain C 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 C:  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 C residue 89 type sequence G description binding site for residue ATP C 401 source : AC3 2) chain C residue 91 type sequence G description binding site for residue ATP C 401 source : AC3 3) chain C residue 92 type sequence S description binding site for residue ATP C 401 source : AC3 4) chain C residue 94 type sequence S description binding site for residue ATP C 401 source : AC3 5) chain C residue 96 type sequence V description binding site for residue ATP C 401 source : AC3 6) chain C residue 109 type sequence A description binding site for residue ATP C 401 source : AC3 7) chain C residue 111 type sequence K description binding site for residue ATP C 401 source : AC3 8) chain C residue 160 type sequence S description binding site for residue ATP C 401 source : AC3 9) chain C residue 162 type sequence A description binding site for residue ATP C 401 source : AC3 10) chain C residue 166 type sequence E description binding site for residue ATP C 401 source : AC3 11) chain C residue 209 type sequence E description binding site for residue ATP C 401 source : AC3 12) chain C residue 212 type sequence L description binding site for residue ATP C 401 source : AC3 13) chain C residue 144 type sequence K description binding site for residue CL C 402 source : AC4 14) chain C residue 131 type sequence R description binding site for Di-peptide PHE E 11 and SEP E 12 source : AC6 15) chain C residue 148 type sequence T description binding site for Di-peptide PHE E 11 and SEP E 12 source : AC6 16) chain C residue 149 type sequence F description binding site for Di-peptide PHE E 11 and SEP E 12 source : AC6 17) chain C residue 150 type sequence Q description binding site for Di-peptide PHE E 11 and SEP E 12 source : AC6 18) chain C residue 145 type sequence L description binding site for Di-peptide SEP E 12 and TYR E 13 source : AC7 19) chain C residue 147 type sequence F description binding site for Di-peptide SEP E 12 and TYR E 13 source : AC7 20) chain C residue 148 type sequence T description binding site for Di-peptide SEP E 12 and TYR E 13 source : AC7 21) chain C residue 150 type sequence Q description binding site for Di-peptide SEP E 12 and TYR E 13 source : AC7 22) chain C 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 23) chain C 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 24) chain C 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 25) chain C 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 26) chain C 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 27) chain C 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 28) chain C residue 209 type BINDING sequence E description BINDING => ECO:0000269|PubMed:22999883 source Swiss-Prot : SWS_FT_FI3 29) chain C 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 30) chain C residue 304 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q9Z2A0 source Swiss-Prot : SWS_FT_FI5 31) chain C 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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