eF-site ID 4yxs-AI PDB Code 4yxs Chain A, I click to enlarge Title CAMP-DEPENDENT PROTEIN KINASE PKA CATALYTIC SUBUNIT WITH PKI-5-24 Classification TRANSFERASE/INHIBITOR Compound cAMP-dependent protein kinase catalytic subunit alpha Source Bos taurus (Bovine) (IPKA_RABIT) Sequence A:  SVKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGS FGRVMLVKHMETGNHYAMKILDKQKVVKLKQIEHTLNEKR ILQAVNFPFLVKLEFSFKDNSNLYMVMEYVPGGEMFSHLR RIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLL IDQQGYIQVTDFGFAKRVKGRTWXLCGTPEYLAPEIILSK GYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSG KVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKDGVNDIKN HKWFATTDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEE EIRVXINEKCGKEFSEF I:  TTYADFIASGRTGRRNAIHD Description (1)  CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA (E.C.2.7.11.11), CAMP-DEPENDENT PROTEIN KINASE INHIBITOR ALPHA Functional site 1) chain A residue 49 type sequence L description binding site for residue EMU A 401 source : AC1 2) chain A residue 70 type sequence A description binding site for residue EMU A 401 source : AC1 3) chain A residue 104 type sequence V description binding site for residue EMU A 401 source : AC1 4) chain A residue 120 type sequence M description binding site for residue EMU A 401 source : AC1 5) chain A residue 121 type sequence E description binding site for residue EMU A 401 source : AC1 6) chain A residue 123 type sequence V description binding site for residue EMU A 401 source : AC1 7) chain A residue 127 type sequence E description binding site for residue EMU A 401 source : AC1 8) chain A residue 170 type sequence E description binding site for residue EMU A 401 source : AC1 9) chain A residue 171 type sequence N description binding site for residue EMU A 401 source : AC1 10) chain A residue 173 type sequence L description binding site for residue EMU A 401 source : AC1 11) chain A residue 183 type sequence T description binding site for residue EMU A 401 source : AC1 12) chain A residue 327 type sequence F description binding site for residue EMU A 401 source : AC1 13) chain I residue 18 type sequence R description binding site for residue EMU A 401 source : AC1 14) chain A residue 166 type catalytic sequence D description 757 source MCSA : MCSA1 15) chain A residue 168 type catalytic sequence K description 757 source MCSA : MCSA1 16) chain A residue 171 type catalytic sequence N description 757 source MCSA : MCSA1 17) chain A residue 184 type catalytic sequence D description 757 source MCSA : MCSA1 18) chain A residue 201 type catalytic sequence T description 757 source MCSA : MCSA1 19) chain A residue 49 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 20) chain A residue 72 type BINDING sequence K description 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_FI3 22) chain A residue 168 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI3 23) chain I residue 15 type SITE sequence R description Important for inhibition source Swiss-Prot : SWS_FT_FI1 24) chain I residue 18 type SITE sequence R description Important for inhibition source Swiss-Prot : SWS_FT_FI1 25) chain I residue 19 type SITE sequence R description Important for inhibition source Swiss-Prot : SWS_FT_FI1 26) chain A residue 49-72 type prosite sequence LGTGSFGRVMLVKHMETGNHYAMK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGSFGRVMlVkhmetgnh..........YAMK source prosite : PS00107 27) chain A residue 162-174 type prosite sequence LIYRDLKPENLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiYrDLKpeNLLI source prosite : PS00108 28) chain A residue 338 type MOD_RES sequence X description Phosphoserine => ECO:0000269|PubMed:6262777 source Swiss-Prot : SWS_FT_FI10 29) chain A residue 48 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P17612 source Swiss-Prot : SWS_FT_FI6 30) chain A residue 195 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P17612 source Swiss-Prot : SWS_FT_FI6 31) chain A residue 139 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI7 32) chain A residue 197 type MOD_RES sequence X description Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:6262777 source Swiss-Prot : SWS_FT_FI8 33) chain A residue 330 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI9

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