eF-site ID 6c9j-ABC PDB Code 6c9j Chain A, B, 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 A:  GSVKIGHYILGDTLGVGTFGKVKVGKHELTGHKVAVKILN RQKIRSLDVVGKIRREIQNLKLFRHPHIIKLYQVISTPSD IFMVMEYVSGGELFDYICKNGRLDEKESRRLFQQILSGVD YCHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNMMSDGE FLRXSCGSPNYAAPEVISGRLYAGPEVDIWSSGVILYALL CGTLPFDDDHVPTLFKKICDGIFYTPQYLNPSVISLLKHM LQVDPMKRATIKDIREHEWFKQDLPKYLFPETRPHPERVP FLVAKAKWHLGIRSQSRPNDIMAEVCRAIKQLDYEWKVVN PYYLRVRRKNPVTSTYSKMSLQLYQVDSRTYLLDFRSIDD ELTPRPGSHTIEFFEMCANLIKILAQ B:  PAQARPTVFRWTGGGKEVYLSGSFNNWSKLPLTRDHNNFV AILDLPEGEHQYKFFVDGQWTHDPSEPIVTSQLGTVNNII QVKKTDFEVFDALMVDSQQEPYVCRAPPILPPHLLQVILN KDTGISCDPALLPEPNHVMLNHLYALSIKDGVMVLSATHR YKKKYVTTLLYKPI C:  NSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALV TNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQ IYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSL IRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPK PEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRV SALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKA LQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDE NDVVKGIVSLSDILQALVLT Description Functional site 1) chain A residue 13 type sequence V description binding site for residue R34 A 601 source : AC1 2) chain A residue 20 type sequence L description binding site for residue R34 A 601 source : AC1 3) chain A residue 31 type sequence K description binding site for residue R34 A 601 source : AC1 4) chain A residue 33 type sequence K description binding site for residue R34 A 601 source : AC1 5) chain A residue 50 type sequence N description binding site for residue R34 A 601 source : AC1 6) chain A residue 53 type sequence K description binding site for residue R34 A 601 source : AC1 7) chain A residue 90 type sequence D description binding site for residue R34 A 601 source : AC1 8) chain B residue 83 type sequence R description binding site for residue R34 A 601 source : AC1 9) chain B residue 106 type sequence T description binding site for residue R34 A 601 source : AC1 10) chain B residue 108 type sequence D description binding site for residue R34 A 601 source : AC1 11) chain B residue 113 type sequence V description binding site for residue R34 A 601 source : AC1 12) chain B residue 115 type sequence I description binding site for residue R34 A 601 source : AC1 13) chain A residue 24 type sequence L description binding site for residue STU A 602 source : AC2 14) chain A residue 25 type sequence G description binding site for residue STU A 602 source : AC2 15) chain A residue 26 type sequence V description binding site for residue STU A 602 source : AC2 16) chain A residue 27 type sequence G description binding site for residue STU A 602 source : AC2 17) chain A residue 45 type sequence A description binding site for residue STU A 602 source : AC2 18) chain A residue 95 type sequence M description binding site for residue STU A 602 source : AC2 19) chain A residue 96 type sequence E description binding site for residue STU A 602 source : AC2 20) chain A residue 97 type sequence Y description binding site for residue STU A 602 source : AC2 21) chain A residue 98 type sequence V description binding site for residue STU A 602 source : AC2 22) chain A residue 102 type sequence E description binding site for residue STU A 602 source : AC2 23) chain A residue 145 type sequence E description binding site for residue STU A 602 source : AC2 24) chain A residue 146 type sequence N description binding site for residue STU A 602 source : AC2 25) chain A residue 148 type sequence L description binding site for residue STU A 602 source : AC2 26) chain A residue 159 type sequence D description binding site for residue STU A 602 source : AC2 27) chain C residue 150 type sequence H description binding site for residue AMP C 401 source : AC3 28) chain C residue 199 type sequence T description binding site for residue AMP C 401 source : AC3 29) chain C residue 203 type sequence I description binding site for residue AMP C 401 source : AC3 30) chain C residue 204 type sequence A description binding site for residue AMP C 401 source : AC3 31) chain C residue 224 type sequence V description binding site for residue AMP C 401 source : AC3 32) chain C residue 225 type sequence S description binding site for residue AMP C 401 source : AC3 33) chain C residue 226 type sequence A description binding site for residue AMP C 401 source : AC3 34) chain C residue 228 type sequence P description binding site for residue AMP C 401 source : AC3 35) chain C residue 311 type sequence I description binding site for residue AMP C 401 source : AC3 36) chain C residue 313 type sequence S description binding site for residue AMP C 401 source : AC3 37) chain C residue 315 type sequence S description binding site for residue AMP C 401 source : AC3 38) chain C residue 316 type sequence D description binding site for residue AMP C 401 source : AC3 39) chain A residue 359 type MOD_RES sequence T description Phosphothreonine; by ULK1 => ECO:0000250|UniProtKB:P54645 source Swiss-Prot : SWS_FT_FI9 40) chain A residue 24-47 type prosite sequence LGVGTFGKVKVGKHELTGHKVAVK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGVGTFGKVKvGkheltghk..........VAVK source prosite : PS00107 41) chain A residue 137-149 type prosite sequence VVHRDLKPENVLL description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvHrDLKpeNVLL source prosite : PS00108 42) 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 43) 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 44) 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 45) 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 46) 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 47) 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 48) chain C residue 260 type MOD_RES sequence S description Phosphoserine; by ULK1 => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI3 49) chain C residue 269 type MOD_RES sequence S description Phosphoserine; by ULK1 => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI3 50) chain C residue 262 type MOD_RES sequence T description Phosphothreonine; by ULK1 => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI4 51) chain B residue 171 type MOD_RES sequence Q description Phosphoserine => ECO:0000250|UniProtKB:Q9R078 source Swiss-Prot : SWS_FT_FI5 52) chain A residue 533 type MOD_RES sequence H description Phosphoserine => ECO:0000250|UniProtKB:Q9R078 source Swiss-Prot : SWS_FT_FI5 53) chain C residue 69 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 54) chain C residue 84 type BINDING sequence M description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 55) chain C residue 129 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 56) chain C residue 151 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 57) chain C residue 169 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 58) chain C residue 241 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 59) chain C residue 268 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 60) chain C residue 276 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P80385 source Swiss-Prot : SWS_FT_FI1 61) chain A residue 458 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19369195 source Swiss-Prot : SWS_FT_FI12 62) chain A residue 531 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI13 63) chain A residue 535 type MOD_RES sequence I description Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI14 64) chain A residue 541 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI15

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