eF-site ID 6c9j-C PDB Code 6c9j Chain C click to enlarge Title 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:  NSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALV TNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQ IYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSL IRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPK PEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRV SALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKA LQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDE NDVVKGIVSLSDILQALVLT Description Functional site 1) chain C residue 150 type sequence H description binding site for residue AMP C 401 source : AC3 2) chain C residue 199 type sequence T description binding site for residue AMP C 401 source : AC3 3) chain C residue 203 type sequence I description binding site for residue AMP C 401 source : AC3 4) chain C residue 204 type sequence A description binding site for residue AMP C 401 source : AC3 5) chain C residue 224 type sequence V description binding site for residue AMP C 401 source : AC3 6) chain C residue 225 type sequence S description binding site for residue AMP C 401 source : AC3 7) chain C residue 226 type sequence A description binding site for residue AMP C 401 source : AC3 8) chain C residue 228 type sequence P description binding site for residue AMP C 401 source : AC3 9) chain C residue 311 type sequence I description binding site for residue AMP C 401 source : AC3 10) chain C residue 313 type sequence S description binding site for residue AMP C 401 source : AC3 11) chain C residue 315 type sequence S description binding site for residue AMP C 401 source : AC3 12) chain C residue 316 type sequence D description binding site for residue AMP C 401 source : AC3 13) chain C residue 69 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 14) chain C residue 84 type BINDING sequence M description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 15) chain C residue 129 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 16) chain C residue 151 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 17) chain C residue 169 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 18) chain C residue 241 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 19) chain C residue 268 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 20) chain C residue 276 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 21) 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 22) 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 23) 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 24) 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 25) 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 26) 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 27) chain C residue 260 type MOD_RES sequence S description Phosphoserine; by ULK1 => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI3 28) chain C residue 269 type MOD_RES sequence S description Phosphoserine; by ULK1 => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI3 29) chain C residue 262 type MOD_RES sequence T description Phosphothreonine; by ULK1 => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI4

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