eF-site ID 6c9h-ABC PDB Code 6c9h Chain A, B, C 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 B:  PAQARPTVFRWTGGGKEVYLSGSFNNWSKLPLTRDHNNFV AILDLPEGEHQYKFFVDGQWTHDPSEPIVTSQLGTVNNII QVKKTDFEVFDALMVDSQRAPPILPPHLLQVILNKDTGIS CDPALLPEPNHVMLNHLYALSIKDGVMVLSATHRYKKKYV TTLLYKPI C:  SVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVT NGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQI YELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLI RNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKP EFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVS ALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKAL QHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDEN DVVKGIVSLSDILQALVLT 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 B residue 83 type sequence R description binding site for residue R34 A 601 source : AC1 9) chain B residue 106 type sequence T description binding site for residue R34 A 601 source : AC1 10) chain B residue 108 type sequence D description binding site for residue R34 A 601 source : AC1 11) chain B residue 111 type sequence N description binding site for residue R34 A 601 source : AC1 12) chain B residue 113 type sequence V description binding site for residue R34 A 601 source : AC1 13) chain A residue 24 type sequence L description binding site for residue STU A 602 source : AC2 14) chain A residue 25 type sequence G description binding site for residue STU A 602 source : AC2 15) chain A residue 26 type sequence V description binding site for residue STU A 602 source : AC2 16) chain A residue 45 type sequence A description binding site for residue STU A 602 source : AC2 17) chain A residue 47 type sequence K description binding site for residue STU A 602 source : AC2 18) chain A residue 95 type sequence M description binding site for residue STU A 602 source : AC2 19) chain A residue 96 type sequence E description binding site for residue STU A 602 source : AC2 20) chain A residue 97 type sequence Y description binding site for residue STU A 602 source : AC2 21) chain A residue 98 type sequence V description binding site for residue STU A 602 source : AC2 22) chain A residue 101 type sequence G description binding site for residue STU A 602 source : AC2 23) chain A residue 102 type sequence E description binding site for residue STU A 602 source : AC2 24) chain A residue 145 type sequence E description binding site for residue STU A 602 source : AC2 25) chain A residue 146 type sequence N description binding site for residue STU A 602 source : AC2 26) chain A residue 148 type sequence L description binding site for residue STU A 602 source : AC2 27) chain A residue 159 type sequence D description binding site for residue STU A 602 source : AC2 28) chain C residue 84 type sequence M description binding site for residue AMP C 1101 source : AC3 29) chain C residue 86 type sequence T description binding site for residue AMP C 1101 source : AC3 30) chain C residue 88 type sequence T description binding site for residue AMP C 1101 source : AC3 31) chain C residue 89 type sequence D description binding site for residue AMP C 1101 source : AC3 32) chain C residue 127 type sequence P description binding site for residue AMP C 1101 source : AC3 33) chain C residue 128 type sequence L description binding site for residue AMP C 1101 source : AC3 34) chain C residue 129 type sequence V description binding site for residue AMP C 1101 source : AC3 35) chain C residue 150 type sequence H description binding site for residue AMP C 1101 source : AC3 36) chain C residue 151 type sequence R description binding site for residue AMP C 1101 source : AC3 37) chain C residue 153 type sequence P description binding site for residue AMP C 1101 source : AC3 38) chain A residue 364 type sequence E description binding site for residue AMP C 1102 source : AC4 39) chain C residue 69 type sequence R description binding site for residue AMP C 1102 source : AC4 40) chain C residue 169 type sequence K description binding site for residue AMP C 1102 source : AC4 41) chain C residue 239 type sequence I description binding site for residue AMP C 1102 source : AC4 42) chain C residue 241 type sequence S description binding site for residue AMP C 1102 source : AC4 43) chain C residue 243 type sequence F description binding site for residue AMP C 1102 source : AC4 44) chain C residue 244 type sequence D description binding site for residue AMP C 1102 source : AC4 45) chain C residue 268 type sequence R description binding site for residue AMP C 1102 source : AC4 46) chain C residue 275 type sequence V description binding site for residue AMP C 1102 source : AC4 47) chain C residue 276 type sequence L description binding site for residue AMP C 1102 source : AC4 48) chain C residue 296 type sequence V description binding site for residue AMP C 1102 source : AC4 49) chain C residue 297 type sequence H description binding site for residue AMP C 1102 source : AC4 50) chain C residue 298 type sequence R description binding site for residue AMP C 1102 source : AC4 51) chain C residue 150 type sequence H description binding site for residue AMP C 1103 source : AC5 52) chain C residue 199 type sequence T description binding site for residue AMP C 1103 source : AC5 53) chain C residue 202 type sequence N description binding site for residue AMP C 1103 source : AC5 54) chain C residue 204 type sequence A description binding site for residue AMP C 1103 source : AC5 55) chain C residue 224 type sequence V description binding site for residue AMP C 1103 source : AC5 56) chain C residue 225 type sequence S description binding site for residue AMP C 1103 source : AC5 57) chain C residue 226 type sequence A description binding site for residue AMP C 1103 source : AC5 58) chain C residue 228 type sequence P description binding site for residue AMP C 1103 source : AC5 59) chain C residue 297 type sequence H description binding site for residue AMP C 1103 source : AC5 60) chain C residue 313 type sequence S description binding site for residue AMP C 1103 source : AC5 61) chain C residue 315 type sequence S description binding site for residue AMP C 1103 source : AC5 62) chain C residue 316 type sequence D description binding site for residue AMP C 1103 source : AC5 63) chain A residue 24-47 type prosite sequence LGVGTFGKVKVGKHELTGHKVAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGVGTFGKVKvGkheltghk..........VAVK source prosite : PS00107 64) chain A residue 137-149 type prosite sequence VVHRDLKPENVLL description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvHrDLKpeNVLL source prosite : PS00108 65) chain C residue 69 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 66) chain C residue 84 type BINDING sequence M description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 67) chain C residue 129 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 68) chain C residue 151 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 69) chain C residue 169 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 70) chain C residue 241 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 71) chain C residue 268 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 72) chain C residue 276 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 73) chain A residue 458 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI12 74) 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 75) 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 76) 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 77) chain C residue 150 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17452784, ECO:0000269|PubMed:24352254, ECO:0000269|PubMed:25412657, ECO:0007744|PDB:4CFF source Swiss-Prot : SWS_FT_FI2 78) chain C residue 199 type BINDING sequence T description BINDING => ECO:0000269|PubMed:17452784, ECO:0000269|PubMed:24352254, ECO:0000269|PubMed:25412657, ECO:0007744|PDB:4CFF source Swiss-Prot : SWS_FT_FI2 79) chain C residue 204 type BINDING sequence A description BINDING => ECO:0000269|PubMed:17452784, ECO:0000269|PubMed:24352254, ECO:0000269|PubMed:25412657, ECO:0007744|PDB:4CFF source Swiss-Prot : SWS_FT_FI2 80) chain C residue 225 type BINDING sequence S description BINDING => ECO:0000269|PubMed:17452784, ECO:0000269|PubMed:24352254, ECO:0000269|PubMed:25412657, ECO:0007744|PDB:4CFF source Swiss-Prot : SWS_FT_FI2 81) chain C residue 297 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17452784, ECO:0000269|PubMed:24352254, ECO:0000269|PubMed:25412657, ECO:0007744|PDB:4CFF source Swiss-Prot : SWS_FT_FI2 82) chain C residue 313 type BINDING sequence S description BINDING => ECO:0000269|PubMed:17452784, ECO:0000269|PubMed:24352254, ECO:0000269|PubMed:25412657, ECO:0007744|PDB:4CFF source Swiss-Prot : SWS_FT_FI2 83) chain C residue 260 type MOD_RES sequence S description Phosphoserine; by ULK1 => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI3 84) chain C residue 269 type MOD_RES sequence S description Phosphoserine; by ULK1 => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI3 85) chain C residue 262 type MOD_RES sequence T description Phosphothreonine; by ULK1 => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI4 86) chain A residue 533 type MOD_RES sequence H description Phosphoserine => ECO:0000250|UniProtKB:Q9R078 source Swiss-Prot : SWS_FT_FI5 87) chain A residue 346 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 88) chain A residue 347 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI7 89) chain A residue 359 type MOD_RES sequence T description Phosphothreonine; by ULK1 => ECO:0000250|UniProtKB:P54645 source Swiss-Prot : SWS_FT_FI9

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