eF-site ID 5n36-A PDB Code 5n36 Chain A click to enlarge Title cAMP-dependent Protein Kinase A from Cricetulus griseus in complex with fragment like molecule 3H-isoindol-2-ium-1-amine Classification TRANSFERASE Compound cAMP-dependent protein kinase catalytic subunit alpha Source (5N36) Sequence A:  GHMGNAAAAKKGXEQESVKEFLAKAKEEFLKKWESPNTAQ LDHFDRIKTLGTGSFGRVMLVKHKETGNHYAMKILDKQKV VKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMV MEYVPGGEMFSHLRRIGRFXEPHARFYAAQIVLTFEYLHS LDLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWXLC GTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF ADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTK RFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKFK GPGDTSNFDDYEEEEIRVXINEKCGKEFTEF Description Functional site 1) chain A residue 15 type sequence V description binding site for residue MPD A 401 source : AC1 2) chain A residue 152 type sequence L description binding site for residue MPD A 401 source : AC1 3) chain A residue 155 type sequence E description binding site for residue MPD A 401 source : AC1 4) chain A residue 306 type sequence Y description binding site for residue MPD A 401 source : AC1 5) chain A residue 57 type sequence V description binding site for residue F05 A 402 source : AC2 6) chain A residue 120 type sequence M description binding site for residue F05 A 402 source : AC2 7) chain A residue 127 type sequence E description binding site for residue F05 A 402 source : AC2 8) chain A residue 170 type sequence E description binding site for residue F05 A 402 source : AC2 9) chain A residue 171 type sequence N description binding site for residue F05 A 402 source : AC2 10) chain A residue 183 type sequence T description binding site for residue F05 A 402 source : AC2 11) chain A residue 184 type sequence D description binding site for residue F05 A 402 source : AC2 12) chain A residue 197 type MOD_RES sequence X description Phosphothreonine; by PDPK1 => ECO:0000250|UniProtKB:P00517 source Swiss-Prot : SWS_FT_FI7 13) chain A residue 49-72 type prosite sequence LGTGSFGRVMLVKHKETGNHYAMK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGSFGRVMlVkhketgnh..........YAMK source prosite : PS00107 14) chain A residue 162-174 type prosite sequence LIYRDLKPENLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiYrDLKpeNLLI source prosite : PS00108 15) chain A residue 166 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 1 type LIPID sequence G description N-myristoyl glycine => ECO:0000250|UniProtKB:P17612 source Swiss-Prot : SWS_FT_FI10 17) chain A residue 2 type MOD_RES sequence N description Deamidated asparagine => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 49 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 19) chain A residue 72 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 20) chain A residue 121 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 168 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 10 type MOD_RES sequence X description Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI4 23) chain A residue 48 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P17612 source Swiss-Prot : SWS_FT_FI5 24) chain A residue 195 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P17612 source Swiss-Prot : SWS_FT_FI5 25) chain A residue 139 type MOD_RES sequence X description Phosphoserine => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI6 26) chain A residue 330 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI8 27) chain A residue 338 type MOD_RES sequence X description Phosphoserine => ECO:0000250|UniProtKB:P00517 source Swiss-Prot : SWS_FT_FI9

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