eF-site ID 5lvp-B PDB Code 5lvp Chain B 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 B:  PRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKIL EKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDE KLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSAL EYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSXF 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 B residue 89 type sequence G description binding site for residue ATP B 401 source : AC2 2) chain B residue 91 type sequence G description binding site for residue ATP B 401 source : AC2 3) chain B residue 92 type sequence S description binding site for residue ATP B 401 source : AC2 4) chain B residue 94 type sequence S description binding site for residue ATP B 401 source : AC2 5) chain B residue 96 type sequence V description binding site for residue ATP B 401 source : AC2 6) chain B residue 109 type sequence A description binding site for residue ATP B 401 source : AC2 7) chain B residue 111 type sequence K description binding site for residue ATP B 401 source : AC2 8) chain B residue 160 type sequence S description binding site for residue ATP B 401 source : AC2 9) chain B residue 162 type sequence A description binding site for residue ATP B 401 source : AC2 10) chain B residue 166 type sequence E description binding site for residue ATP B 401 source : AC2 11) chain B residue 212 type sequence L description binding site for residue ATP B 401 source : AC2 12) chain B residue 131 type sequence R description binding site for Di-peptide PHE G 11 and SEP G 12 source : AD1 13) chain B residue 148 type sequence T description binding site for Di-peptide PHE G 11 and SEP G 12 source : AD1 14) chain B residue 150 type sequence Q description binding site for Di-peptide PHE G 11 and SEP G 12 source : AD1 15) chain B residue 157 type sequence F description binding site for Di-peptide PHE G 11 and SEP G 12 source : AD1 16) chain B residue 147 type sequence F description binding site for Di-peptide SEP G 12 and TYR G 13 source : AD2 17) chain B residue 148 type sequence T description binding site for Di-peptide SEP G 12 and TYR G 13 source : AD2 18) chain B residue 150 type sequence Q description binding site for Di-peptide SEP G 12 and TYR G 13 source : AD2 19) chain B 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 20) chain B 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 21) chain B 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 22) chain B 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 23) chain B 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 24) chain B 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 25) chain B residue 209 type BINDING sequence E description BINDING => ECO:0000269|PubMed:22999883 source Swiss-Prot : SWS_FT_FI3 26) chain B 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 27) chain B residue 304 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q9Z2A0 source Swiss-Prot : SWS_FT_FI5 28) chain B 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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