eF-site ID 6i2d-A PDB Code 6i2d Chain A click to enlarge Title Crystal Structure of the Protein-Kinase A catalytic subunit from Cricetulus Griseus in complex with compounds RKp182 and RKp117 Classification TRANSFERASE Compound cAMP-dependent protein kinase catalytic subunit alpha Source (G3HK48_CRIGR) Sequence A:  KGXEQESVKEFLAKAKEEFLKKWESPSQNTAQLDHFDRIK TLGTGSFGRVMLVKHKETGNHYAMKILDKQKVVKLKQIEH TLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVMEYVPGGE MFSHLRRIGRFXEPHARFYAAQIVLTFEYLHSLDLIYRDL KPENLLIDQQGYIQVTDFGFAKRVKGRTWXLCGTPEYLAP EIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIY EKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNG VNDIKNHKWFATTDWIAIYQRKVEAPFIPKFKGPGDTSNF DDYEEEEIRVXINEKCGKEFTEF 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 51 type sequence T description binding site for residue 9LQ A 401 source : AC1 2) chain A residue 52 type sequence G description binding site for residue 9LQ A 401 source : AC1 3) chain A residue 57 type sequence V description binding site for residue 9LQ A 401 source : AC1 4) chain A residue 70 type sequence A description binding site for residue 9LQ A 401 source : AC1 5) chain A residue 72 type sequence K description binding site for residue 9LQ A 401 source : AC1 6) chain A residue 121 type sequence E description binding site for residue 9LQ A 401 source : AC1 7) chain A residue 122 type sequence Y description binding site for residue 9LQ A 401 source : AC1 8) chain A residue 123 type sequence V description binding site for residue 9LQ A 401 source : AC1 9) chain A residue 173 type sequence L description binding site for residue 9LQ A 401 source : AC1 10) chain A residue 184 type sequence D description binding site for residue 9LQ A 401 source : AC1 11) chain A residue 49-72 type prosite sequence LGTGSFGRVMLVKHKETGNHYAMK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGSFGRVMlVkhketgnh..........YAMK source prosite : PS00107 12) chain A residue 162-174 type prosite sequence LIYRDLKPENLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiYrDLKpeNLLI source prosite : PS00108 13) chain A residue 195 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P17612 source Swiss-Prot : SWS_FT_FI5 14) chain A residue 48 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P17612 source Swiss-Prot : SWS_FT_FI5 15) chain A residue 139 type MOD_RES sequence X description Phosphoserine => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI6 16) chain A residue 197 type MOD_RES sequence X description Phosphothreonine; by PDPK1 => ECO:0000250|UniProtKB:P00517 source Swiss-Prot : SWS_FT_FI7 17) chain A residue 330 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI8 18) chain A residue 338 type MOD_RES sequence X description Phosphoserine => ECO:0000250|UniProtKB:P00517 source Swiss-Prot : SWS_FT_FI9 19) 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 20) chain A residue 72 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 121 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 168 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 23) chain A residue 49 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 24) chain A residue 10 type MOD_RES sequence X description Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI4

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