eF-site ID 4cfh-ABCE PDB Code 4cfh Chain A, B, C, E click to enlarge Title Structure of an active form of mammalian AMPK Classification TRANSFERASE Compound 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-1 Source (AAKG1_RAT) Sequence A:  RVKIGHYILGDTLGVGTFGKVKVGKHELTGHKVAVKILNR QKIRSLDVVGKIRREIQNLKLFRHPHIIKLYQVISTPSDI FMVMEYVSGGELFDYICKNGRLDEKESRRLFQQILSGVDY CHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNMMSDGEF LRXSCGSPNYAAPEVISGRLYAGPEVDIWSSGVILYALLC GTLPFDDDHVPTLFKKICDGIFYTPQYLNPSVISLLKHML QVDPMKRATIKDIREHEWFKQDLPKYLFPEDAVAYHLIID NRRIMNEAKDFYLATSPPDSFLDDHHLTRPHPERVPFLVA ETPRAAKWHLGIRSQSRPNDIMAEVCRAIKQLDYEWKVVN PYYLRVRRKNPVTSTFSKMSLQLYQVDSRTYLLDFRSIDD EI B:  KSPPILPPHLLQVILNKDTNISCDPALLPEPNHVMLNHLY ALSIKDSVMVLSATHRYKKKYVTTLLYKP C:  PGSHTIEFFEMCANLIKILAQ E:  NSSVYTTFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFAL VTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALV QIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSS LIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFP KPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHR VSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTK ALQHRSHYFEGVLKCYLHETLEAIINRLVEAEVHRLVVVD EHDVVKGIVSLSDILQALVLT Description Functional site 1) chain E residue 69 type sequence R description BINDING SITE FOR RESIDUE AMP E 1325 source : AC1 2) chain E residue 169 type sequence K description BINDING SITE FOR RESIDUE AMP E 1325 source : AC1 3) chain E residue 239 type sequence I description BINDING SITE FOR RESIDUE AMP E 1325 source : AC1 4) chain E residue 241 type sequence S description BINDING SITE FOR RESIDUE AMP E 1325 source : AC1 5) chain E residue 243 type sequence F description BINDING SITE FOR RESIDUE AMP E 1325 source : AC1 6) chain E residue 244 type sequence D description BINDING SITE FOR RESIDUE AMP E 1325 source : AC1 7) chain E residue 268 type sequence R description BINDING SITE FOR RESIDUE AMP E 1325 source : AC1 8) chain E residue 275 type sequence V description BINDING SITE FOR RESIDUE AMP E 1325 source : AC1 9) chain E residue 276 type sequence L description BINDING SITE FOR RESIDUE AMP E 1325 source : AC1 10) chain E residue 296 type sequence V description BINDING SITE FOR RESIDUE AMP E 1325 source : AC1 11) chain E residue 297 type sequence H description BINDING SITE FOR RESIDUE AMP E 1325 source : AC1 12) chain E residue 298 type sequence R description BINDING SITE FOR RESIDUE AMP E 1325 source : AC1 13) chain E residue 150 type sequence H description BINDING SITE FOR RESIDUE AMP E 1326 source : AC2 14) chain E residue 199 type sequence T description BINDING SITE FOR RESIDUE AMP E 1326 source : AC2 15) chain E residue 203 type sequence I description BINDING SITE FOR RESIDUE AMP E 1326 source : AC2 16) chain E residue 204 type sequence A description BINDING SITE FOR RESIDUE AMP E 1326 source : AC2 17) chain E residue 224 type sequence V description BINDING SITE FOR RESIDUE AMP E 1326 source : AC2 18) chain E residue 225 type sequence S description BINDING SITE FOR RESIDUE AMP E 1326 source : AC2 19) chain E residue 226 type sequence A description BINDING SITE FOR RESIDUE AMP E 1326 source : AC2 20) chain E residue 297 type sequence H description BINDING SITE FOR RESIDUE AMP E 1326 source : AC2 21) chain E residue 311 type sequence I description BINDING SITE FOR RESIDUE AMP E 1326 source : AC2 22) chain E residue 313 type sequence S description BINDING SITE FOR RESIDUE AMP E 1326 source : AC2 23) chain E residue 315 type sequence S description BINDING SITE FOR RESIDUE AMP E 1326 source : AC2 24) chain E residue 316 type sequence D description BINDING SITE FOR RESIDUE AMP E 1326 source : AC2 25) chain A residue 22 type sequence L description BINDING SITE FOR RESIDUE STU A 1550 source : AC3 26) chain A residue 23 type sequence G description BINDING SITE FOR RESIDUE STU A 1550 source : AC3 27) chain A residue 24 type sequence V description BINDING SITE FOR RESIDUE STU A 1550 source : AC3 28) chain A residue 25 type sequence G description BINDING SITE FOR RESIDUE STU A 1550 source : AC3 29) chain A residue 43 type sequence A description BINDING SITE FOR RESIDUE STU A 1550 source : AC3 30) chain A residue 45 type sequence K description BINDING SITE FOR RESIDUE STU A 1550 source : AC3 31) chain A residue 93 type sequence M description BINDING SITE FOR RESIDUE STU A 1550 source : AC3 32) chain A residue 94 type sequence E description BINDING SITE FOR RESIDUE STU A 1550 source : AC3 33) chain A residue 95 type sequence Y description BINDING SITE FOR RESIDUE STU A 1550 source : AC3 34) chain A residue 96 type sequence V description BINDING SITE FOR RESIDUE STU A 1550 source : AC3 35) chain A residue 99 type sequence G description BINDING SITE FOR RESIDUE STU A 1550 source : AC3 36) chain A residue 100 type sequence E description BINDING SITE FOR RESIDUE STU A 1550 source : AC3 37) chain A residue 143 type sequence E description BINDING SITE FOR RESIDUE STU A 1550 source : AC3 38) chain A residue 144 type sequence N description BINDING SITE FOR RESIDUE STU A 1550 source : AC3 39) chain A residue 146 type sequence L description BINDING SITE FOR RESIDUE STU A 1550 source : AC3 40) chain A residue 157 type sequence D description BINDING SITE FOR RESIDUE STU A 1550 source : AC3 41) chain E residue 69 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 42) chain E residue 84 type BINDING sequence M description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 43) chain E residue 129 type BINDING sequence V description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 44) chain E residue 151 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 45) chain E residue 169 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 46) chain E residue 241 type BINDING sequence S description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 47) chain E residue 268 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 48) chain E residue 276 type BINDING sequence L description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 49) chain E residue 150 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17851531, ECO:0000269|PubMed:21399626, ECO:0007744|PDB:2V8Q, ECO:0007744|PDB:2Y8L source Swiss-Prot : SWS_FT_FI2 50) chain E residue 199 type BINDING sequence T description BINDING => ECO:0000269|PubMed:17851531, ECO:0000269|PubMed:21399626, ECO:0007744|PDB:2V8Q, ECO:0007744|PDB:2Y8L source Swiss-Prot : SWS_FT_FI2 51) chain E residue 204 type BINDING sequence A description BINDING => ECO:0000269|PubMed:17851531, ECO:0000269|PubMed:21399626, ECO:0007744|PDB:2V8Q, ECO:0007744|PDB:2Y8L source Swiss-Prot : SWS_FT_FI2 52) chain E residue 225 type BINDING sequence S description BINDING => ECO:0000269|PubMed:17851531, ECO:0000269|PubMed:21399626, ECO:0007744|PDB:2V8Q, ECO:0007744|PDB:2Y8L source Swiss-Prot : SWS_FT_FI2 53) chain E residue 297 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17851531, ECO:0000269|PubMed:21399626, ECO:0007744|PDB:2V8Q, ECO:0007744|PDB:2Y8L source Swiss-Prot : SWS_FT_FI2 54) chain E residue 313 type BINDING sequence S description BINDING => ECO:0000269|PubMed:17851531, ECO:0000269|PubMed:21399626, ECO:0007744|PDB:2V8Q, ECO:0007744|PDB:2Y8L source Swiss-Prot : SWS_FT_FI2 55) chain E residue 260 type MOD_RES sequence S description Phosphoserine; by ULK1 => ECO:0000305|PubMed:21460634 source Swiss-Prot : SWS_FT_FI3 56) chain A residue 344 type MOD_RES sequence T description Phosphoserine; by ULK1 => ECO:0000305|PubMed:21460634 source Swiss-Prot : SWS_FT_FI3 57) chain A residue 371 type MOD_RES sequence T description Phosphoserine; by ULK1 => ECO:0000305|PubMed:21460634 source Swiss-Prot : SWS_FT_FI3 58) chain E residue 262 type MOD_RES sequence T description Phosphothreonine; by ULK1 => ECO:0000305|PubMed:21460634 source Swiss-Prot : SWS_FT_FI4 59) chain E residue 269 type MOD_RES sequence S description Phosphoserine; by ULK1 => ECO:0000269|PubMed:21460634 source Swiss-Prot : SWS_FT_FI5 60) chain A residue 345 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q13131 source Swiss-Prot : SWS_FT_FI6 61) chain A residue 456 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q13131 source Swiss-Prot : SWS_FT_FI6 62) chain A residue 349 type MOD_RES sequence S description Phosphoserine; by ULK1 => ECO:0000305|PubMed:21460634 source Swiss-Prot : SWS_FT_FI7 63) chain A residue 357 type MOD_RES sequence T description Phosphothreonine; by ULK1 => ECO:0000305|PubMed:21460634 source Swiss-Prot : SWS_FT_FI8 64) chain A residue 22-45 type prosite sequence LGVGTFGKVKVGKHELTGHKVAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGVGTFGKVKvGkheltghk..........VAVK source prosite : PS00107 65) chain A residue 135-147 type prosite sequence VVHRDLKPENVLL description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvHrDLKpeNVLL source prosite : PS00108

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