eF-site ID 4qfr-C PDB Code 4qfr Chain C click to enlarge Title Structure of AMPK in complex with Cl-A769662 activator and STAUROSPORINE inhibitor Classification signaling protein/inhibitor/activator Compound 5'-AMP-activated protein kinase catalytic subunit alpha-1 Source Rattus norvegicus (Rat) (AAKG1_RAT) Sequence C:  YTTFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNG VRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYE LEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRN KIHRLPVIDPESGNTLYILTHKRILKFLKLFITSLEELQI GTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVV DIYSKFDVINLAAEKTYNNLDVSVTKALQHRVLKCYLHET LEAIINRLVEAEVHRLVVVDEHDVVKGIVSLSDILQALV 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 C residue 150 type sequence H description BINDING SITE FOR RESIDUE AMP C 401 source : AC7 2) chain C residue 199 type sequence T description BINDING SITE FOR RESIDUE AMP C 401 source : AC7 3) chain C residue 203 type sequence I description BINDING SITE FOR RESIDUE AMP C 401 source : AC7 4) chain C residue 204 type sequence A description BINDING SITE FOR RESIDUE AMP C 401 source : AC7 5) chain C residue 224 type sequence V description BINDING SITE FOR RESIDUE AMP C 401 source : AC7 6) chain C residue 225 type sequence S description BINDING SITE FOR RESIDUE AMP C 401 source : AC7 7) chain C residue 226 type sequence A description BINDING SITE FOR RESIDUE AMP C 401 source : AC7 8) chain C residue 297 type sequence H description BINDING SITE FOR RESIDUE AMP C 401 source : AC7 9) chain C residue 298 type sequence R description BINDING SITE FOR RESIDUE AMP C 401 source : AC7 10) chain C residue 311 type sequence I description BINDING SITE FOR RESIDUE AMP C 401 source : AC7 11) chain C residue 313 type sequence S description BINDING SITE FOR RESIDUE AMP C 401 source : AC7 12) chain C residue 315 type sequence S description BINDING SITE FOR RESIDUE AMP C 401 source : AC7 13) chain C residue 316 type sequence D description BINDING SITE FOR RESIDUE AMP C 401 source : AC7 14) chain C residue 69 type sequence R description BINDING SITE FOR RESIDUE AMP C 402 source : AC8 15) chain C residue 169 type sequence K description BINDING SITE FOR RESIDUE AMP C 402 source : AC8 16) chain C residue 239 type sequence I description BINDING SITE FOR RESIDUE AMP C 402 source : AC8 17) chain C residue 241 type sequence S description BINDING SITE FOR RESIDUE AMP C 402 source : AC8 18) chain C residue 243 type sequence F description BINDING SITE FOR RESIDUE AMP C 402 source : AC8 19) chain C residue 244 type sequence D description BINDING SITE FOR RESIDUE AMP C 402 source : AC8 20) chain C residue 268 type sequence R description BINDING SITE FOR RESIDUE AMP C 402 source : AC8 21) chain C residue 276 type sequence L description BINDING SITE FOR RESIDUE AMP C 402 source : AC8 22) chain C residue 296 type sequence V description BINDING SITE FOR RESIDUE AMP C 402 source : AC8 23) chain C residue 297 type sequence H description BINDING SITE FOR RESIDUE AMP C 402 source : AC8 24) chain C residue 298 type sequence R description BINDING SITE FOR RESIDUE AMP C 402 source : AC8 25) chain C residue 69 type sequence R description BINDING SITE FOR RESIDUE ADP C 403 source : AC9 26) chain C residue 84 type sequence M description BINDING SITE FOR RESIDUE ADP C 403 source : AC9 27) chain C residue 86 type sequence T description BINDING SITE FOR RESIDUE ADP C 403 source : AC9 28) chain C residue 88 type sequence T description BINDING SITE FOR RESIDUE ADP C 403 source : AC9 29) chain C residue 89 type sequence D description BINDING SITE FOR RESIDUE ADP C 403 source : AC9 30) chain C residue 120 type sequence Y description BINDING SITE FOR RESIDUE ADP C 403 source : AC9 31) chain C residue 127 type sequence P description BINDING SITE FOR RESIDUE ADP C 403 source : AC9 32) chain C residue 129 type sequence V description BINDING SITE FOR RESIDUE ADP C 403 source : AC9 33) chain C residue 149 type sequence I description BINDING SITE FOR RESIDUE ADP C 403 source : AC9 34) chain C residue 150 type sequence H description BINDING SITE FOR RESIDUE ADP C 403 source : AC9 35) chain C residue 151 type sequence R description BINDING SITE FOR RESIDUE ADP C 403 source : AC9 36) chain C residue 153 type sequence P description BINDING SITE FOR RESIDUE ADP C 403 source : AC9 37) chain C residue 151 type sequence R description BINDING SITE FOR RESIDUE SO4 C 404 source : BC1 38) chain C residue 167 type sequence T description BINDING SITE FOR RESIDUE SO4 C 404 source : BC1 39) chain C residue 169 type sequence K description BINDING SITE FOR RESIDUE SO4 C 404 source : BC1 40) chain C residue 69 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 41) chain C residue 84 type BINDING sequence M description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 42) chain C residue 129 type BINDING sequence V description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 43) chain C residue 151 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 44) chain C residue 169 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 45) chain C residue 241 type BINDING sequence S description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 46) chain C residue 268 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 47) chain C residue 276 type BINDING sequence L description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 48) 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 49) 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 50) 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 51) 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 52) 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 53) 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 54) chain C residue 260 type MOD_RES sequence S description Phosphoserine; by ULK1 => ECO:0000305|PubMed:21460634 source Swiss-Prot : SWS_FT_FI3 55) chain C residue 262 type MOD_RES sequence T description Phosphothreonine; by ULK1 => ECO:0000305|PubMed:21460634 source Swiss-Prot : SWS_FT_FI4

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