eF-site ID 6e4u-ABC PDB Code 6e4u Chain A, B, C click to enlarge Title Structure of AMPK bound to activator Classification TRANSFERASE Compound 5'-AMP-activated protein kinase catalytic subunit alpha-1 Source (AAKG1_RAT) Sequence A:  GRVKIGHYILGDTLGVGTFGKVKVGKHELTGHKVAVKILN RQKIRSLDVVGKIRREIQNLKLFRHPHIIKLYQVISTPSD IFMVMEYVSGGELFDYICKNGRLDEKESRRLFQQILSGVD YCHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNMMSDGE FLRXSCGSPNYAAPEVISGRLYAGPEVDIWSSGVILYALL CGTLPFDDDHVPTLFKKICDGIFYTPQYLNPSVISLLKHM LQVDPMKRATIKDIREHEWFKQDLPKYLFPEKWHLGIRSQ SRPNDIMAEVCRAIKQLDYEWKVVNPYYLRVRRKNPVTST FSKMSLQLYQVDSRTYLLDFRSIDDPGSHTIEFFEMCANL IKILAQ B:  ARPTVFRWTGGGKEVYLSGSFNNWSKLPLTRXQNNFVAIL DLPEGEHQYKFFVDGQWTHDPSEPIVTSQLGTVNNIIQVK KTDFEVFDALMVDSQKAPPILPPHLLQVILNKSCDPALLP EPNHVMLNHLYALSIKDGVMVLSATHRYKKKYVTTLLYKP I C:  SVYTTFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVT NGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQI YELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLI RNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFSLE ELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEK GRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRVLKCY LHETLEAIINRLVEAEVHRLVVVDEHDVVKGIVSLSDILQ ALV Description (1)  5'-AMP-activated protein kinase catalytic subunit alpha-1,5'-AMP-activated protein kinase catalytic subunit alpha-1 (E.C.2.7.11.1,2.7.11.1,2.7.11.27,2.7.11.31,2.7.11.26), 5'-AMP-activated protein kinase subunit beta-1, 5'-AMP-activated protein kinase subunit gamma-1 Functional site 1) chain A residue 22 type sequence L description binding site for residue STU A 601 source : AC1 2) chain A residue 23 type sequence G description binding site for residue STU A 601 source : AC1 3) chain A residue 24 type sequence V description binding site for residue STU A 601 source : AC1 4) chain A residue 25 type sequence G description binding site for residue STU A 601 source : AC1 5) chain A residue 30 type sequence V description binding site for residue STU A 601 source : AC1 6) chain A residue 43 type sequence A description binding site for residue STU A 601 source : AC1 7) chain A residue 94 type sequence E description binding site for residue STU A 601 source : AC1 8) chain A residue 95 type sequence Y description binding site for residue STU A 601 source : AC1 9) chain A residue 96 type sequence V description binding site for residue STU A 601 source : AC1 10) chain A residue 99 type sequence G description binding site for residue STU A 601 source : AC1 11) chain A residue 100 type sequence E description binding site for residue STU A 601 source : AC1 12) chain A residue 143 type sequence E description binding site for residue STU A 601 source : AC1 13) chain A residue 144 type sequence N description binding site for residue STU A 601 source : AC1 14) chain A residue 146 type sequence L description binding site for residue STU A 601 source : AC1 15) chain A residue 156 type sequence A description binding site for residue STU A 601 source : AC1 16) chain A residue 157 type sequence D description binding site for residue STU A 601 source : AC1 17) chain A residue 18 type sequence L description binding site for residue HU7 A 602 source : AC2 18) chain A residue 19 type sequence G description binding site for residue HU7 A 602 source : AC2 19) chain A residue 29 type sequence K description binding site for residue HU7 A 602 source : AC2 20) chain A residue 31 type sequence K description binding site for residue HU7 A 602 source : AC2 21) chain A residue 46 type sequence I description binding site for residue HU7 A 602 source : AC2 22) chain A residue 88 type sequence D description binding site for residue HU7 A 602 source : AC2 23) chain B residue 83 type sequence R description binding site for residue HU7 A 602 source : AC2 24) chain B residue 110 type sequence N description binding site for residue HU7 A 602 source : AC2 25) chain B residue 111 type sequence N description binding site for residue HU7 A 602 source : AC2 26) chain B residue 113 type sequence V description binding site for residue HU7 A 602 source : AC2 27) chain B residue 115 type sequence I description binding site for residue HU7 A 602 source : AC2 28) chain A residue 97 type sequence S description binding site for residue CL A 603 source : AC3 29) chain A residue 149 type sequence A description binding site for residue CL A 603 source : AC3 30) chain A residue 210 type sequence G description binding site for residue CL A 604 source : AC4 31) chain A residue 24 type sequence V description binding site for residue CL A 605 source : AC5 32) chain A residue 34 type sequence K description binding site for residue CL A 606 source : AC6 33) chain A residue 41 type sequence K description binding site for residue CL A 606 source : AC6 34) chain C residue 150 type sequence H description binding site for residue AMP C 401 source : AC7 35) chain C residue 199 type sequence T description binding site for residue AMP C 401 source : AC7 36) chain C residue 203 type sequence I description binding site for residue AMP C 401 source : AC7 37) chain C residue 204 type sequence A description binding site for residue AMP C 401 source : AC7 38) chain C residue 224 type sequence V description binding site for residue AMP C 401 source : AC7 39) chain C residue 225 type sequence S description binding site for residue AMP C 401 source : AC7 40) chain C residue 226 type sequence A description binding site for residue AMP C 401 source : AC7 41) chain C residue 311 type sequence I description binding site for residue AMP C 401 source : AC7 42) chain C residue 313 type sequence S description binding site for residue AMP C 401 source : AC7 43) chain C residue 315 type sequence S description binding site for residue AMP C 401 source : AC7 44) chain C residue 316 type sequence D description binding site for residue AMP C 401 source : AC7 45) chain C residue 69 type sequence R description binding site for residue AMP C 402 source : AC8 46) chain C residue 239 type sequence I description binding site for residue AMP C 402 source : AC8 47) chain C residue 241 type sequence S description binding site for residue AMP C 402 source : AC8 48) chain C residue 243 type sequence F description binding site for residue AMP C 402 source : AC8 49) chain C residue 244 type sequence D description binding site for residue AMP C 402 source : AC8 50) chain C residue 268 type sequence R description binding site for residue AMP C 402 source : AC8 51) chain C residue 276 type sequence L description binding site for residue AMP C 402 source : AC8 52) chain C residue 296 type sequence V description binding site for residue AMP C 402 source : AC8 53) chain C residue 297 type sequence H description binding site for residue AMP C 402 source : AC8 54) chain C residue 298 type sequence R description binding site for residue AMP C 402 source : AC8 55) chain C residue 69 type sequence R description binding site for residue ADP C 403 source : AC9 56) chain C residue 84 type sequence M description binding site for residue ADP C 403 source : AC9 57) chain C residue 86 type sequence T description binding site for residue ADP C 403 source : AC9 58) chain C residue 88 type sequence T description binding site for residue ADP C 403 source : AC9 59) chain C residue 89 type sequence D description binding site for residue ADP C 403 source : AC9 60) chain C residue 120 type sequence Y description binding site for residue ADP C 403 source : AC9 61) chain C residue 127 type sequence P description binding site for residue ADP C 403 source : AC9 62) chain C residue 128 type sequence L description binding site for residue ADP C 403 source : AC9 63) chain C residue 129 type sequence V description binding site for residue ADP C 403 source : AC9 64) chain C residue 149 type sequence I description binding site for residue ADP C 403 source : AC9 65) chain C residue 150 type sequence H description binding site for residue ADP C 403 source : AC9 66) chain C residue 151 type sequence R description binding site for residue ADP C 403 source : AC9 67) chain C residue 242 type sequence K description binding site for residue ADP C 403 source : AC9 68) chain C residue 151 type sequence R description binding site for residue SO4 C 404 source : AD1 69) chain C residue 167 type sequence T description binding site for residue SO4 C 404 source : AD1 70) chain C residue 169 type sequence K description binding site for residue SO4 C 404 source : AD1 71) chain C residue 297 type sequence H description binding site for residue SO4 C 404 source : AD1 72) chain A residue 135-147 type prosite sequence VVHRDLKPENVLL description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvHrDLKpeNVLL source prosite : PS00108 73) chain A residue 22-45 type prosite sequence LGVGTFGKVKVGKHELTGHKVAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGVGTFGKVKvGkheltghk..........VAVK source prosite : PS00107 74) chain C residue 262 type MOD_RES sequence T description Phosphothreonine; by ULK1 => ECO:0000305|PubMed:21460634 source Swiss-Prot : SWS_FT_FI4 75) chain C residue 129 type BINDING sequence V description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 76) chain C residue 151 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 77) chain C residue 169 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 78) chain C residue 241 type BINDING sequence S description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 79) chain C residue 268 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 80) chain C residue 276 type BINDING sequence L description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 81) chain C residue 69 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 82) chain C residue 84 type BINDING sequence M description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 83) chain C 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 84) chain C 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 85) chain C 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 86) chain C 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 87) chain C 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 88) chain C 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 89) chain C residue 260 type MOD_RES sequence S description Phosphoserine; by ULK1 => ECO:0000305|PubMed:21460634 source Swiss-Prot : SWS_FT_FI3 90) chain A residue 456 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q13131 source Swiss-Prot : SWS_FT_FI6

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