eF-site ID 6c9h-C PDB Code 6c9h Chain 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 C:  SVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVT NGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQI YELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLI RNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKP EFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVS ALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKAL QHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDEN DVVKGIVSLSDILQALVLT Description Functional site 1) chain C residue 84 type sequence M description binding site for residue AMP C 1101 source : AC3 2) chain C residue 86 type sequence T description binding site for residue AMP C 1101 source : AC3 3) chain C residue 88 type sequence T description binding site for residue AMP C 1101 source : AC3 4) chain C residue 89 type sequence D description binding site for residue AMP C 1101 source : AC3 5) chain C residue 127 type sequence P description binding site for residue AMP C 1101 source : AC3 6) chain C residue 128 type sequence L description binding site for residue AMP C 1101 source : AC3 7) chain C residue 129 type sequence V description binding site for residue AMP C 1101 source : AC3 8) chain C residue 150 type sequence H description binding site for residue AMP C 1101 source : AC3 9) chain C residue 151 type sequence R description binding site for residue AMP C 1101 source : AC3 10) chain C residue 153 type sequence P description binding site for residue AMP C 1101 source : AC3 11) chain C residue 69 type sequence R description binding site for residue AMP C 1102 source : AC4 12) chain C residue 169 type sequence K description binding site for residue AMP C 1102 source : AC4 13) chain C residue 239 type sequence I description binding site for residue AMP C 1102 source : AC4 14) chain C residue 241 type sequence S description binding site for residue AMP C 1102 source : AC4 15) chain C residue 243 type sequence F description binding site for residue AMP C 1102 source : AC4 16) chain C residue 244 type sequence D description binding site for residue AMP C 1102 source : AC4 17) chain C residue 268 type sequence R description binding site for residue AMP C 1102 source : AC4 18) chain C residue 275 type sequence V description binding site for residue AMP C 1102 source : AC4 19) chain C residue 276 type sequence L description binding site for residue AMP C 1102 source : AC4 20) chain C residue 296 type sequence V description binding site for residue AMP C 1102 source : AC4 21) chain C residue 297 type sequence H description binding site for residue AMP C 1102 source : AC4 22) chain C residue 298 type sequence R description binding site for residue AMP C 1102 source : AC4 23) chain C residue 150 type sequence H description binding site for residue AMP C 1103 source : AC5 24) chain C residue 199 type sequence T description binding site for residue AMP C 1103 source : AC5 25) chain C residue 202 type sequence N description binding site for residue AMP C 1103 source : AC5 26) chain C residue 204 type sequence A description binding site for residue AMP C 1103 source : AC5 27) chain C residue 224 type sequence V description binding site for residue AMP C 1103 source : AC5 28) chain C residue 225 type sequence S description binding site for residue AMP C 1103 source : AC5 29) chain C residue 226 type sequence A description binding site for residue AMP C 1103 source : AC5 30) chain C residue 228 type sequence P description binding site for residue AMP C 1103 source : AC5 31) chain C residue 297 type sequence H description binding site for residue AMP C 1103 source : AC5 32) chain C residue 313 type sequence S description binding site for residue AMP C 1103 source : AC5 33) chain C residue 315 type sequence S description binding site for residue AMP C 1103 source : AC5 34) chain C residue 316 type sequence D description binding site for residue AMP C 1103 source : AC5 35) 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 36) 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 37) 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 38) 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 39) 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 40) 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 41) chain C residue 260 type MOD_RES sequence S description Phosphoserine; by ULK1 => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI3 42) chain C residue 269 type MOD_RES sequence S description Phosphoserine; by ULK1 => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI3 43) chain C residue 262 type MOD_RES sequence T description Phosphothreonine; by ULK1 => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI4 44) chain C residue 69 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 45) chain C residue 84 type BINDING sequence M description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 46) chain C residue 129 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 47) chain C residue 151 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 48) chain C residue 169 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 49) chain C residue 241 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 50) chain C residue 268 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 51) chain C residue 276 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1

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