eF-site ID 4qfg-C PDB Code 4qfg Chain C click to enlarge Title Structure of AMPK in complex with STAUROSPORINE inhibitor and in the absence of a synthetic activator Classification signaling protein/inhibitor Compound 5'-AMP-activated protein kinase catalytic subunit alpha-1 Source null (AAKG1_RAT) Sequence C:  SSVYTTFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALV TNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQ IYELEEHKIETWREVYLQPLVCISPNASLFDAVSSLIRNK IHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFM SKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALP VVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHR LKCYLHETLEAIINRLVEAEVHRLVVVDEHDVVKGIVSLS DILQALV 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 : 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 298 type sequence R 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 86 type sequence T description BINDING SITE FOR RESIDUE SO4 C 402 source : AC7 14) chain C residue 87 type sequence I description BINDING SITE FOR RESIDUE SO4 C 402 source : AC7 15) chain C residue 88 type sequence T description BINDING SITE FOR RESIDUE SO4 C 402 source : AC7 16) chain C residue 150 type sequence H description BINDING SITE FOR RESIDUE SO4 C 402 source : AC7 17) chain C residue 151 type sequence R description BINDING SITE FOR RESIDUE SO4 C 402 source : AC7 18) chain C residue 241 type sequence S description BINDING SITE FOR RESIDUE SO4 C 403 source : AC8 19) chain C residue 243 type sequence F description BINDING SITE FOR RESIDUE SO4 C 403 source : AC8 20) chain C residue 297 type sequence H description BINDING SITE FOR RESIDUE SO4 C 403 source : AC8 21) chain C residue 298 type sequence R description BINDING SITE FOR RESIDUE SO4 C 403 source : AC8 22) chain C residue 260 type MOD_RES sequence S description Phosphoserine; by ULK1 => ECO:0000305|PubMed:21460634 source Swiss-Prot : SWS_FT_FI3 23) chain C residue 262 type MOD_RES sequence T description Phosphothreonine; by ULK1 => ECO:0000305|PubMed:21460634 source Swiss-Prot : SWS_FT_FI4 24) chain C residue 129 type BINDING sequence V description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 25) chain C residue 151 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 26) chain C residue 169 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 27) chain C residue 241 type BINDING sequence S description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 28) chain C residue 268 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 29) chain C residue 276 type BINDING sequence L description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 30) chain C residue 69 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 31) chain C residue 84 type BINDING sequence M description BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92 source Swiss-Prot : SWS_FT_FI1 32) 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 33) 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 34) 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 35) 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 36) 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 37) 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

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