eF-site ID 4qfg-ABC PDB Code 4qfg Chain A, B, C click to enlarge Title Structure of AMPK in complex with STAUROSPORINE inhibitor and in the absence of a synthetic activator Classification signaling protein/inhibitor Compound 5'-AMP-activated protein kinase catalytic subunit alpha-1 Source Rattus norvegicus (Rat) (AAKG1_RAT) Sequence A:  GRVKIGHYILGDTLGVGTFGKVKVGKHELTGHKVAVKILN RQKIRSLDVVGKIRREIQNLKLFRHPHIIKLYQVISTPSD IFMVMEYVSGGELFDYICKNGRLDEKESRRLFQQILSGVD YCHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNMMSDGE FLRXSCGSPNYAAPEVISGRLYAGPEVDIWSSGVILYALL CGTLPFDDDHVPTLFKKICDGIFYTPQYLNPSVISLLKHM LQVDPMKRATIKDIREHEWFKQDLPKYLFPWHLGIRSQSR PNDIMAEVCRAIKQLDYEWKVVNPYYLRVRRKNPVTSTFS KMSLQLYQVDSRTYLLDFRSIDDERPGSHTIEFFEMCANL IKILAQ B:  ARPTVFRWTGGGKEVYLSGSFNNWSKLPLTRDQNNFVAIL DLPEGEHQYKFFVDGQWTHDPSEPIVTSQLGTVNNIIQVK KTDFEVFDALMVDSQKAPPILPPHLLQVILNKSCDPALLP EPNHVMLNHLYALSIKDGVMVLSATHRYKKKYVTTLLYKP I C:  SSVYTTFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALV TNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQ IYELEEHKIETWREVYLQPLVCISPNASLFDAVSSLIRNK IHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFM SKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALP VVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHR LKCYLHETLEAIINRLVEAEVHRLVVVDEHDVVKGIVSLS DILQALV Description (1)  5'-AMP-activated protein kinase catalytic subunit alpha-1 (E.C.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 25 type sequence G description BINDING SITE FOR RESIDUE STU A 601 source : AC1 4) chain A residue 30 type sequence V description BINDING SITE FOR RESIDUE STU A 601 source : AC1 5) chain A residue 43 type sequence A description BINDING SITE FOR RESIDUE STU A 601 source : AC1 6) chain A residue 77 type sequence I 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 24 type sequence V description BINDING SITE FOR RESIDUE CL A 602 source : AC2 18) chain A residue 34 type sequence K description BINDING SITE FOR RESIDUE CL A 603 source : AC3 19) chain A residue 41 type sequence K description BINDING SITE FOR RESIDUE CL A 603 source : AC3 20) chain A residue 97 type sequence S description BINDING SITE FOR RESIDUE CL A 604 source : AC4 21) chain A residue 149 type sequence A description BINDING SITE FOR RESIDUE CL A 604 source : AC4 22) chain A residue 29 type sequence K description BINDING SITE FOR RESIDUE SO4 A 605 source : AC5 23) chain A residue 48 type sequence N description BINDING SITE FOR RESIDUE SO4 A 605 source : AC5 24) chain A residue 51 type sequence K description BINDING SITE FOR RESIDUE SO4 A 605 source : AC5 25) chain B residue 83 type sequence R description BINDING SITE FOR RESIDUE SO4 A 605 source : AC5 26) chain B residue 110 type sequence N description BINDING SITE FOR RESIDUE SO4 A 605 source : AC5 27) chain C residue 150 type sequence H description BINDING SITE FOR RESIDUE AMP C 401 source : AC6 28) chain C residue 199 type sequence T description BINDING SITE FOR RESIDUE AMP C 401 source : AC6 29) chain C residue 203 type sequence I description BINDING SITE FOR RESIDUE AMP C 401 source : AC6 30) chain C residue 204 type sequence A description BINDING SITE FOR RESIDUE AMP C 401 source : AC6 31) chain C residue 224 type sequence V description BINDING SITE FOR RESIDUE AMP C 401 source : AC6 32) chain C residue 225 type sequence S description BINDING SITE FOR RESIDUE AMP C 401 source : AC6 33) chain C residue 226 type sequence A description BINDING SITE FOR RESIDUE AMP C 401 source : AC6 34) chain C residue 298 type sequence R description BINDING SITE FOR RESIDUE AMP C 401 source : AC6 35) chain C residue 311 type sequence I description BINDING SITE FOR RESIDUE AMP C 401 source : AC6 36) chain C residue 313 type sequence S description BINDING SITE FOR RESIDUE AMP C 401 source : AC6 37) chain C residue 315 type sequence S description BINDING SITE FOR RESIDUE AMP C 401 source : AC6 38) chain C residue 316 type sequence D description BINDING SITE FOR RESIDUE AMP C 401 source : AC6 39) chain C residue 86 type sequence T description BINDING SITE FOR RESIDUE SO4 C 402 source : AC7 40) chain C residue 87 type sequence I description BINDING SITE FOR RESIDUE SO4 C 402 source : AC7 41) chain C residue 88 type sequence T description BINDING SITE FOR RESIDUE SO4 C 402 source : AC7 42) chain C residue 150 type sequence H description BINDING SITE FOR RESIDUE SO4 C 402 source : AC7 43) chain C residue 151 type sequence R description BINDING SITE FOR RESIDUE SO4 C 402 source : AC7 44) chain C residue 241 type sequence S description BINDING SITE FOR RESIDUE SO4 C 403 source : AC8 45) chain C residue 243 type sequence F description BINDING SITE FOR RESIDUE SO4 C 403 source : AC8 46) chain C residue 297 type sequence H description BINDING SITE FOR RESIDUE SO4 C 403 source : AC8 47) chain C residue 298 type sequence R description BINDING SITE FOR RESIDUE SO4 C 403 source : AC8 48) chain A residue 532 type MOD_RES sequence T description Phosphoserine => ECO:0000269|PubMed:12764152, ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI12 49) chain C residue 69 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 50) chain C residue 84 type BINDING sequence M description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 51) chain C residue 129 type BINDING sequence V description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 52) chain C residue 151 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 53) chain C residue 169 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 54) chain C residue 241 type BINDING sequence S description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 55) chain C residue 268 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 56) chain C residue 276 type BINDING sequence L description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 57) chain C residue 260 type MOD_RES sequence S description Phosphoserine; by ULK1 => ECO:0000305|PubMed:21460634 source Swiss-Prot : SWS_FT_FI3 58) chain A residue 22-45 type prosite sequence LGVGTFGKVKVGKHELTGHKVAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGVGTFGKVKvGkheltghk..........VAVK source prosite : PS00107 59) chain A residue 135-147 type prosite sequence VVHRDLKPENVLL description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvHrDLKpeNVLL source prosite : PS00108 60) 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 61) 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 62) 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 63) 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 64) 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 65) 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 66) chain C residue 262 type MOD_RES sequence T description Phosphothreonine; by ULK1 => ECO:0000305|PubMed:21460634 source Swiss-Prot : SWS_FT_FI4 67) chain A residue 456 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q13131 source Swiss-Prot : SWS_FT_FI6 68) chain A residue 544 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:Q13131 source Swiss-Prot : SWS_FT_FI6

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