eF-site ID 5lvp-ABCDEFGH PDB Code 5lvp Chain A, B, C, D, E, F, G, H 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 B:  PRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKIL EKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDE KLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSAL EYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSXF VGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPF RAGNEGLIFAKIIKLEYDFPEKFFPKARDLVEKLLVLDAT KRLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLT C:  RKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILE KRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEK LYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALE YLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLNXFV GTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFR AGNEGLIFAKIIKLEYDFPEKFFPKARDLVEKLLVLDATK RLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLT D:  PRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKIL EKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDE KLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSAL EYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLNXF VGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPF RAGNEGLIFAKIIKLEYDFPEKFFPKARDLVEKLLVLDAT KRLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLT E:  FPQFXYS F:  FPQFXYSA G:  FPQFXYSA H:  FPQFXYS 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 B residue 89 type sequence G description binding site for residue ATP B 401 source : AC2 13) chain B residue 91 type sequence G description binding site for residue ATP B 401 source : AC2 14) chain B residue 92 type sequence S description binding site for residue ATP B 401 source : AC2 15) chain B residue 94 type sequence S description binding site for residue ATP B 401 source : AC2 16) chain B residue 96 type sequence V description binding site for residue ATP B 401 source : AC2 17) chain B residue 109 type sequence A description binding site for residue ATP B 401 source : AC2 18) chain B residue 111 type sequence K description binding site for residue ATP B 401 source : AC2 19) chain B residue 160 type sequence S description binding site for residue ATP B 401 source : AC2 20) chain B residue 162 type sequence A description binding site for residue ATP B 401 source : AC2 21) chain B residue 166 type sequence E description binding site for residue ATP B 401 source : AC2 22) chain B residue 212 type sequence L description binding site for residue ATP B 401 source : AC2 23) chain C residue 89 type sequence G description binding site for residue ATP C 401 source : AC3 24) chain C residue 91 type sequence G description binding site for residue ATP C 401 source : AC3 25) chain C residue 92 type sequence S description binding site for residue ATP C 401 source : AC3 26) chain C residue 94 type sequence S description binding site for residue ATP C 401 source : AC3 27) chain C residue 96 type sequence V description binding site for residue ATP C 401 source : AC3 28) chain C residue 109 type sequence A description binding site for residue ATP C 401 source : AC3 29) chain C residue 111 type sequence K description binding site for residue ATP C 401 source : AC3 30) chain C residue 160 type sequence S description binding site for residue ATP C 401 source : AC3 31) chain C residue 162 type sequence A description binding site for residue ATP C 401 source : AC3 32) chain C residue 166 type sequence E description binding site for residue ATP C 401 source : AC3 33) chain C residue 209 type sequence E description binding site for residue ATP C 401 source : AC3 34) chain C residue 212 type sequence L description binding site for residue ATP C 401 source : AC3 35) chain C residue 144 type sequence K description binding site for residue CL C 402 source : AC4 36) chain D residue 89 type sequence G description binding site for residue ATP D 500 source : AC5 37) chain D residue 90 type sequence E description binding site for residue ATP D 500 source : AC5 38) chain D residue 91 type sequence G description binding site for residue ATP D 500 source : AC5 39) chain D residue 92 type sequence S description binding site for residue ATP D 500 source : AC5 40) chain D residue 94 type sequence S description binding site for residue ATP D 500 source : AC5 41) chain D residue 96 type sequence V description binding site for residue ATP D 500 source : AC5 42) chain D residue 109 type sequence A description binding site for residue ATP D 500 source : AC5 43) chain D residue 111 type sequence K description binding site for residue ATP D 500 source : AC5 44) chain D residue 160 type sequence S description binding site for residue ATP D 500 source : AC5 45) chain D residue 162 type sequence A description binding site for residue ATP D 500 source : AC5 46) chain D residue 166 type sequence E description binding site for residue ATP D 500 source : AC5 47) chain D residue 212 type sequence L description binding site for residue ATP D 500 source : AC5 48) chain C residue 131 type sequence R description binding site for Di-peptide PHE E 11 and SEP E 12 source : AC6 49) chain C residue 148 type sequence T description binding site for Di-peptide PHE E 11 and SEP E 12 source : AC6 50) chain C residue 149 type sequence F description binding site for Di-peptide PHE E 11 and SEP E 12 source : AC6 51) chain C residue 150 type sequence Q description binding site for Di-peptide PHE E 11 and SEP E 12 source : AC6 52) chain E residue 8 type sequence F description binding site for Di-peptide PHE E 11 and SEP E 12 source : AC6 53) chain E residue 9 type sequence P description binding site for Di-peptide PHE E 11 and SEP E 12 source : AC6 54) chain E residue 10 type sequence Q description binding site for Di-peptide PHE E 11 and SEP E 12 source : AC6 55) chain E residue 13 type sequence Y description binding site for Di-peptide PHE E 11 and SEP E 12 source : AC6 56) chain C residue 145 type sequence L description binding site for Di-peptide SEP E 12 and TYR E 13 source : AC7 57) chain C residue 147 type sequence F description binding site for Di-peptide SEP E 12 and TYR E 13 source : AC7 58) chain C residue 148 type sequence T description binding site for Di-peptide SEP E 12 and TYR E 13 source : AC7 59) chain C residue 150 type sequence Q description binding site for Di-peptide SEP E 12 and TYR E 13 source : AC7 60) chain E residue 8 type sequence F description binding site for Di-peptide SEP E 12 and TYR E 13 source : AC7 61) chain E residue 10 type sequence Q description binding site for Di-peptide SEP E 12 and TYR E 13 source : AC7 62) chain E residue 11 type sequence F description binding site for Di-peptide SEP E 12 and TYR E 13 source : AC7 63) chain E residue 14 type sequence S description binding site for Di-peptide SEP E 12 and TYR E 13 source : AC7 64) chain A residue 131 type sequence R description binding site for Di-peptide PHE F 11 and SEP F 12 source : AC8 65) chain A residue 148 type sequence T description binding site for Di-peptide PHE F 11 and SEP F 12 source : AC8 66) chain A residue 149 type sequence F description binding site for Di-peptide PHE F 11 and SEP F 12 source : AC8 67) chain A residue 150 type sequence Q description binding site for Di-peptide PHE F 11 and SEP F 12 source : AC8 68) chain A residue 157 type sequence F description binding site for Di-peptide PHE F 11 and SEP F 12 source : AC8 69) chain F residue 8 type sequence F description binding site for Di-peptide PHE F 11 and SEP F 12 source : AC8 70) chain F residue 9 type sequence P description binding site for Di-peptide PHE F 11 and SEP F 12 source : AC8 71) chain F residue 10 type sequence Q description binding site for Di-peptide PHE F 11 and SEP F 12 source : AC8 72) chain F residue 13 type sequence Y description binding site for Di-peptide PHE F 11 and SEP F 12 source : AC8 73) chain A residue 135 type sequence S description binding site for Di-peptide SEP F 12 and TYR F 13 source : AC9 74) chain A residue 147 type sequence F description binding site for Di-peptide SEP F 12 and TYR F 13 source : AC9 75) chain A residue 148 type sequence T description binding site for Di-peptide SEP F 12 and TYR F 13 source : AC9 76) chain A residue 150 type sequence Q description binding site for Di-peptide SEP F 12 and TYR F 13 source : AC9 77) chain F residue 9 type sequence P description binding site for Di-peptide SEP F 12 and TYR F 13 source : AC9 78) chain F residue 10 type sequence Q description binding site for Di-peptide SEP F 12 and TYR F 13 source : AC9 79) chain F residue 11 type sequence F description binding site for Di-peptide SEP F 12 and TYR F 13 source : AC9 80) chain F residue 14 type sequence S description binding site for Di-peptide SEP F 12 and TYR F 13 source : AC9 81) chain B residue 131 type sequence R description binding site for Di-peptide PHE G 11 and SEP G 12 source : AD1 82) chain B residue 148 type sequence T description binding site for Di-peptide PHE G 11 and SEP G 12 source : AD1 83) chain B residue 150 type sequence Q description binding site for Di-peptide PHE G 11 and SEP G 12 source : AD1 84) chain B residue 157 type sequence F description binding site for Di-peptide PHE G 11 and SEP G 12 source : AD1 85) chain G residue 8 type sequence F description binding site for Di-peptide PHE G 11 and SEP G 12 source : AD1 86) chain G residue 9 type sequence P description binding site for Di-peptide PHE G 11 and SEP G 12 source : AD1 87) chain G residue 10 type sequence Q description binding site for Di-peptide PHE G 11 and SEP G 12 source : AD1 88) chain G residue 13 type sequence Y description binding site for Di-peptide PHE G 11 and SEP G 12 source : AD1 89) chain B residue 147 type sequence F description binding site for Di-peptide SEP G 12 and TYR G 13 source : AD2 90) chain B residue 148 type sequence T description binding site for Di-peptide SEP G 12 and TYR G 13 source : AD2 91) chain B residue 150 type sequence Q description binding site for Di-peptide SEP G 12 and TYR G 13 source : AD2 92) chain G residue 9 type sequence P description binding site for Di-peptide SEP G 12 and TYR G 13 source : AD2 93) chain G residue 10 type sequence Q description binding site for Di-peptide SEP G 12 and TYR G 13 source : AD2 94) chain G residue 11 type sequence F description binding site for Di-peptide SEP G 12 and TYR G 13 source : AD2 95) chain G residue 14 type sequence S description binding site for Di-peptide SEP G 12 and TYR G 13 source : AD2 96) chain D residue 131 type sequence R description binding site for Di-peptide PHE H 11 and SEP H 12 source : AD3 97) chain D residue 148 type sequence T description binding site for Di-peptide PHE H 11 and SEP H 12 source : AD3 98) chain D residue 149 type sequence F description binding site for Di-peptide PHE H 11 and SEP H 12 source : AD3 99) chain D residue 150 type sequence Q description binding site for Di-peptide PHE H 11 and SEP H 12 source : AD3 100) chain D residue 155 type sequence L description binding site for Di-peptide PHE H 11 and SEP H 12 source : AD3 101) chain D residue 157 type sequence F description binding site for Di-peptide PHE H 11 and SEP H 12 source : AD3 102) chain H residue 8 type sequence F description binding site for Di-peptide PHE H 11 and SEP H 12 source : AD3 103) chain H residue 9 type sequence P description binding site for Di-peptide PHE H 11 and SEP H 12 source : AD3 104) chain H residue 10 type sequence Q description binding site for Di-peptide PHE H 11 and SEP H 12 source : AD3 105) chain H residue 13 type sequence Y description binding site for Di-peptide PHE H 11 and SEP H 12 source : AD3 106) chain D residue 135 type sequence S description binding site for Di-peptide SEP H 12 and TYR H 13 source : AD4 107) chain D residue 145 type sequence L description binding site for Di-peptide SEP H 12 and TYR H 13 source : AD4 108) chain D residue 148 type sequence T description binding site for Di-peptide SEP H 12 and TYR H 13 source : AD4 109) chain D residue 150 type sequence Q description binding site for Di-peptide SEP H 12 and TYR H 13 source : AD4 110) chain H residue 10 type sequence Q description binding site for Di-peptide SEP H 12 and TYR H 13 source : AD4 111) chain H residue 11 type sequence F description binding site for Di-peptide SEP H 12 and TYR H 13 source : AD4 112) chain H residue 14 type sequence S description binding site for Di-peptide SEP H 12 and TYR H 13 source : AD4 113) 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 114) 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 115) 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 116) 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 117) 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 118) 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 119) 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 120) 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 121) 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 122) 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 123) 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 124) 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 125) 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 126) 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 127) 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 128) 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 129) 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 130) 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 131) 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 132) 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 133) 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 134) 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 135) 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 136) 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 137) chain A residue 209 type BINDING sequence E description BINDING => ECO:0000269|PubMed:22999883 source Swiss-Prot : SWS_FT_FI3 138) chain B residue 209 type BINDING sequence E description BINDING => ECO:0000269|PubMed:22999883 source Swiss-Prot : SWS_FT_FI3 139) chain C residue 209 type BINDING sequence E description BINDING => ECO:0000269|PubMed:22999883 source Swiss-Prot : SWS_FT_FI3 140) chain D residue 209 type BINDING sequence E description BINDING => ECO:0000269|PubMed:22999883 source Swiss-Prot : SWS_FT_FI3 141) 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 142) 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 143) 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 144) 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 145) chain A residue 304 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q9Z2A0 source Swiss-Prot : SWS_FT_FI5 146) chain B residue 304 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q9Z2A0 source Swiss-Prot : SWS_FT_FI5 147) chain C residue 304 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q9Z2A0 source Swiss-Prot : SWS_FT_FI5 148) chain D residue 304 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q9Z2A0 source Swiss-Prot : SWS_FT_FI5 149) chain A residue 354 type MOD_RES sequence T description Phosphothreonine; by MELK => ECO:0000269|PubMed:22544756 source Swiss-Prot : SWS_FT_FI6 150) chain B residue 354 type MOD_RES sequence T description Phosphothreonine; by MELK => ECO:0000269|PubMed:22544756 source Swiss-Prot : SWS_FT_FI6 151) chain C residue 354 type MOD_RES sequence T description Phosphothreonine; by MELK => ECO:0000269|PubMed:22544756 source Swiss-Prot : SWS_FT_FI6 152) chain D residue 354 type MOD_RES sequence T description Phosphothreonine; by MELK => ECO:0000269|PubMed:22544756 source Swiss-Prot : SWS_FT_FI6 153) chain A residue 88-111 type prosite sequence LGEGSFSTVVLARELATSREYAIK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGSFSTVVlArelatsre..........YAIK source prosite : PS00107 154) 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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