eF-site ID 6c9h-A PDB Code 6c9h Chain A click to enlarge Title non-phosphorylated AMP-activated protein kinase bound to pharmacological activator R734 Classification TRANSFERASE Compound 5'-AMP-activated protein kinase catalytic subunit alpha-1 Source (AAKG1_HUMAN) Sequence A:  GSVKIGHYILGDTLGVGTFGKVKVGKHELTGHKVAVKILN RQKIRSLDVVGKIRREIQNLKLFRHPHIIKLYQVISTPSD IFMVMEYVSGGELFDYICKNGRLDEKESRRLFQQILSGVD YCHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNMMSDGE FLRTSCGSPNYAAPEVISGRLYAGPEVDIWSSGVILYALL CGTLPFDDDHVPTLFKKICDGIFYTPQYLNPSVISLLKHM LQVDPMKRATIKDIREHEWFKQDLPKYLFPEDPSYSSTMI DDEALKEVLYNRNHQDPLAVAYHLIIDNRRIMNEAKDFYL ATSPTRPHPERVPFKAKWHLGIRSQSRPNDIMAEVCRAIK QLDYEWKVVNPYYLRVRRKNPVTSTYSKMSLQLYQVDSRT YLLDFRSIDDELTPRPGSHTIEFFEMCANLIKILA Description Functional site 1) chain A residue 13 type sequence V description binding site for residue R34 A 601 source : AC1 2) chain A residue 20 type sequence L description binding site for residue R34 A 601 source : AC1 3) chain A residue 29 type sequence F description binding site for residue R34 A 601 source : AC1 4) chain A residue 33 type sequence K description binding site for residue R34 A 601 source : AC1 5) chain A residue 48 type sequence I description binding site for residue R34 A 601 source : AC1 6) chain A residue 50 type sequence N description binding site for residue R34 A 601 source : AC1 7) chain A residue 90 type sequence D description binding site for residue R34 A 601 source : AC1 8) chain A residue 24 type sequence L description binding site for residue STU A 602 source : AC2 9) chain A residue 25 type sequence G description binding site for residue STU A 602 source : AC2 10) chain A residue 26 type sequence V description binding site for residue STU A 602 source : AC2 11) chain A residue 45 type sequence A description binding site for residue STU A 602 source : AC2 12) chain A residue 47 type sequence K description binding site for residue STU A 602 source : AC2 13) chain A residue 95 type sequence M description binding site for residue STU A 602 source : AC2 14) chain A residue 96 type sequence E description binding site for residue STU A 602 source : AC2 15) chain A residue 97 type sequence Y description binding site for residue STU A 602 source : AC2 16) chain A residue 98 type sequence V description binding site for residue STU A 602 source : AC2 17) chain A residue 101 type sequence G description binding site for residue STU A 602 source : AC2 18) chain A residue 102 type sequence E description binding site for residue STU A 602 source : AC2 19) chain A residue 145 type sequence E description binding site for residue STU A 602 source : AC2 20) chain A residue 146 type sequence N description binding site for residue STU A 602 source : AC2 21) chain A residue 148 type sequence L description binding site for residue STU A 602 source : AC2 22) chain A residue 159 type sequence D description binding site for residue STU A 602 source : AC2 23) chain A residue 364 type sequence E description binding site for residue AMP C 1102 source : AC4 24) chain A residue 533 type MOD_RES sequence H description Phosphoserine => ECO:0000250|UniProtKB:Q9R078 source Swiss-Prot : SWS_FT_FI5 25) chain A residue 346 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 26) chain A residue 347 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI7 27) chain A residue 359 type MOD_RES sequence T description Phosphothreonine; by ULK1 => ECO:0000250|UniProtKB:P54645 source Swiss-Prot : SWS_FT_FI9 28) chain A residue 458 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI12 29) chain A residue 531 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI13 30) chain A residue 535 type MOD_RES sequence I description Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI14 31) chain A residue 541 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI15 32) chain A residue 24-47 type prosite sequence LGVGTFGKVKVGKHELTGHKVAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGVGTFGKVKvGkheltghk..........VAVK source prosite : PS00107 33) chain A residue 137-149 type prosite sequence VVHRDLKPENVLL description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvHrDLKpeNVLL source prosite : PS00108

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