eF-site ID 5ouc-AE PDB Code 5ouc Chain A, E click to enlarge Title Crystal Structure of the Protein-Kinase A catalytic subunit from Criteculus Griseus in complex with compounds RKp191 and RKp190 Classification TRANSFERASE Compound cAMP-dependent protein kinase catalytic subunit alpha Source (5OUC) Sequence A:  GHMGNAAAAKKGXEQESVKEFLAKAKEEFLKKWESPSQNT AQLDHFDRIKTLGTGSFGRVMLVKHKETGNHYAMKILDKQ KVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLY MVMEYVPGGEMFSHLRRIGRFXEPHARFYAAQIVLTFEYL HSLDLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWX LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPP FFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDL TKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPK FKGPGDTSNFDDYEEEEIRVXINEKCGKEFTEF E:  TTYADFIASGRTGRRNSI Description (1)  cAMP-dependent protein kinase catalytic subunit alpha (E.C.2.7.11.11), cAMP-dependent protein kinase inhibitor Functional site 1) chain A residue 49-72 type prosite sequence LGTGSFGRVMLVKHKETGNHYAMK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGSFGRVMlVkhketgnh..........YAMK source prosite : PS00107 2) chain A residue 162-174 type prosite sequence LIYRDLKPENLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiYrDLKpeNLLI source prosite : PS00108 3) 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 4) chain A residue 72 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 5) chain A residue 121 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 6) chain A residue 168 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 7) chain A residue 49 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 8) chain A residue 2 type MOD_RES sequence N description Deamidated asparagine => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI3 9) chain A residue 10 type MOD_RES sequence X description Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI4 10) chain A residue 195 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P17612 source Swiss-Prot : SWS_FT_FI5 11) chain A residue 48 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P17612 source Swiss-Prot : SWS_FT_FI5 12) chain A residue 139 type MOD_RES sequence X description Phosphoserine => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI6 13) chain A residue 197 type MOD_RES sequence X description Phosphothreonine; by PDPK1 => ECO:0000250|UniProtKB:P00517 source Swiss-Prot : SWS_FT_FI7 14) chain A residue 330 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI8 15) chain A residue 338 type MOD_RES sequence X description Phosphoserine => ECO:0000250|UniProtKB:P00517 source Swiss-Prot : SWS_FT_FI9 16) chain A residue 1 type LIPID sequence G description N-myristoyl glycine => ECO:0000250|UniProtKB:P17612 source Swiss-Prot : SWS_FT_FI10

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