eF-site ID 6e4w-C PDB Code 6e4w Chain C click to enlarge Title Structure of AMPK bound to activator Classification TRANSFERASE Compound 5'-AMP-activated protein kinase catalytic subunit alpha-1 Source (AAKG1_RAT) Sequence C:  YTTFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNG VRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYE LEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRN KIHRLPVIDPESGNTLYILTHKRILKFLKLFITSLEELQI GTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVV DIYSKFDVINLAAEKTYNNLDVSVTKALQHRLKCYLHETL EAIINRLVEAEVHRLVVVDEHDVVKGIVSLSDILQALV Description (1)  5'-AMP-activated protein kinase catalytic subunit alpha-1,5'-AMP-activated protein kinase catalytic subunit alpha-1 (E.C.2.7.11.1,2.7.11.1,2.7.11.27,2.7.11.31,2.7.11.26), 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 : AC6 2) chain C residue 199 type sequence T description binding site for residue AMP C 401 source : AC6 3) chain C residue 203 type sequence I description binding site for residue AMP C 401 source : AC6 4) chain C residue 204 type sequence A description binding site for residue AMP C 401 source : AC6 5) chain C residue 224 type sequence V description binding site for residue AMP C 401 source : AC6 6) chain C residue 225 type sequence S description binding site for residue AMP C 401 source : AC6 7) chain C residue 226 type sequence A description binding site for residue AMP C 401 source : AC6 8) chain C residue 228 type sequence P description binding site for residue AMP C 401 source : AC6 9) chain C residue 311 type sequence I description binding site for residue AMP C 401 source : AC6 10) chain C residue 313 type sequence S description binding site for residue AMP C 401 source : AC6 11) chain C residue 315 type sequence S description binding site for residue AMP C 401 source : AC6 12) chain C residue 316 type sequence D description binding site for residue AMP C 401 source : AC6 13) chain C residue 69 type sequence R description binding site for residue AMP C 402 source : AC7 14) chain C residue 239 type sequence I description binding site for residue AMP C 402 source : AC7 15) chain C residue 241 type sequence S description binding site for residue AMP C 402 source : AC7 16) chain C residue 243 type sequence F description binding site for residue AMP C 402 source : AC7 17) chain C residue 244 type sequence D description binding site for residue AMP C 402 source : AC7 18) chain C residue 268 type sequence R description binding site for residue AMP C 402 source : AC7 19) chain C residue 276 type sequence L description binding site for residue AMP C 402 source : AC7 20) chain C residue 296 type sequence V description binding site for residue AMP C 402 source : AC7 21) chain C residue 297 type sequence H description binding site for residue AMP C 402 source : AC7 22) chain C residue 298 type sequence R description binding site for residue AMP C 402 source : AC7 23) chain C residue 69 type sequence R description binding site for residue ADP C 403 source : AC8 24) chain C residue 84 type sequence M description binding site for residue ADP C 403 source : AC8 25) chain C residue 86 type sequence T description binding site for residue ADP C 403 source : AC8 26) chain C residue 88 type sequence T description binding site for residue ADP C 403 source : AC8 27) chain C residue 89 type sequence D description binding site for residue ADP C 403 source : AC8 28) chain C residue 120 type sequence Y description binding site for residue ADP C 403 source : AC8 29) chain C residue 127 type sequence P description binding site for residue ADP C 403 source : AC8 30) chain C residue 128 type sequence L description binding site for residue ADP C 403 source : AC8 31) chain C residue 129 type sequence V description binding site for residue ADP C 403 source : AC8 32) chain C residue 149 type sequence I description binding site for residue ADP C 403 source : AC8 33) chain C residue 150 type sequence H description binding site for residue ADP C 403 source : AC8 34) chain C residue 151 type sequence R description binding site for residue ADP C 403 source : AC8 35) chain C residue 153 type sequence P description binding site for residue ADP C 403 source : AC8 36) chain C residue 242 type sequence K description binding site for residue ADP C 403 source : AC8 37) chain C residue 151 type sequence R description binding site for residue SO4 C 404 source : AC9 38) chain C residue 167 type sequence T description binding site for residue SO4 C 404 source : AC9 39) chain C residue 169 type sequence K description binding site for residue SO4 C 404 source : AC9 40) chain C residue 297 type sequence H description binding site for residue SO4 C 404 source : AC9 41) chain C residue 69 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 42) chain C residue 84 type BINDING sequence M description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 43) chain C residue 129 type BINDING sequence V description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 44) chain C residue 151 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 45) chain C residue 169 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 46) chain C residue 241 type BINDING sequence S description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 47) chain C residue 268 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 48) chain C residue 276 type BINDING sequence L description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 49) 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 50) 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 51) 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 52) 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 53) 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 54) 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 55) chain C residue 260 type MOD_RES sequence S description Phosphoserine; by ULK1 => ECO:0000305|PubMed:21460634 source Swiss-Prot : SWS_FT_FI3 56) 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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