eF-site ID 5n32-A PDB Code 5n32 Chain A click to enlarge Title cAMP-dependent Protein Kinase A from Cricetulus griseus in complex with fragment like molecule 4-chlorobenzyl carbamimidothioate Classification TRANSFERASE Compound cAMP-dependent protein kinase catalytic subunit alpha Source (A0A061IH64_CRIGR) Sequence A:  HMGAAAAKKGXEQESVKEFLAKAKEEFLKKWESPNTAQLD HFDRIKTLGTGSFRVMLVKHKETGNHYAMKILDKQKVVKL KQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVMEY VPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDL IYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWXLCGTP EYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQ PIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFG NLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKFKGPG DTSNFDDYEEEEIRVXINEKCGKEFTEF Description Functional site 1) chain A residue 49 type sequence L description binding site for residue 8K5 A 401 source : AC1 2) chain A residue 70 type sequence A description binding site for residue 8K5 A 401 source : AC1 3) chain A residue 121 type sequence E description binding site for residue 8K5 A 401 source : AC1 4) chain A residue 127 type sequence E description binding site for residue 8K5 A 401 source : AC1 5) chain A residue 170 type sequence E description binding site for residue 8K5 A 401 source : AC1 6) chain A residue 171 type sequence N description binding site for residue 8K5 A 401 source : AC1 7) chain A residue 173 type sequence L description binding site for residue 8K5 A 401 source : AC1 8) chain A residue 183 type sequence T description binding site for residue 8K5 A 401 source : AC1 9) chain A residue 327 type sequence F description binding site for residue 8K5 A 401 source : AC1 10) chain A residue 82 type sequence L description binding site for residue 8K5 A 402 source : AC2 11) chain A residue 83 type sequence K description binding site for residue 8K5 A 402 source : AC2 12) chain A residue 135 type sequence I description binding site for residue 8K5 A 402 source : AC2 13) chain A residue 136 type sequence G description binding site for residue 8K5 A 402 source : AC2 14) chain A residue 137 type sequence R description binding site for residue 8K5 A 402 source : AC2 15) chain A residue 197 type sequence X description binding site for residue 8K5 A 402 source : AC2 16) chain A residue 15 type sequence V description binding site for residue MPD A 403 source : AC3 17) chain A residue 100 type sequence F description binding site for residue MPD A 403 source : AC3 18) chain A residue 152 type sequence L description binding site for residue MPD A 403 source : AC3 19) chain A residue 155 type sequence E description binding site for residue MPD A 403 source : AC3 20) chain A residue 306 type sequence Y description binding site for residue MPD A 403 source : AC3 21) chain A residue 49-72 type prosite sequence LGTGSFRVMLVKHKETGNHYAMK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGSFGRVMlVkhketgnh..........YAMK source prosite : PS00107 22) chain A residue 162-174 type prosite sequence LIYRDLKPENLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiYrDLKpeNLLI source prosite : PS00108 23) 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 24) chain A residue 1 type LIPID sequence G description N-myristoyl glycine => ECO:0000250|UniProtKB:P17612 source Swiss-Prot : SWS_FT_FI10 25) chain A residue 49 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 26) chain A residue 72 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 27) chain A residue 121 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 28) chain A residue 168 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 29) chain A residue 10 type MOD_RES sequence X description Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI4 30) chain A residue 48 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P17612 source Swiss-Prot : SWS_FT_FI5 31) chain A residue 195 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P17612 source Swiss-Prot : SWS_FT_FI5 32) chain A residue 139 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI6 33) chain A residue 197 type MOD_RES sequence X description Phosphothreonine; by PDPK1 => ECO:0000250|UniProtKB:P00517 source Swiss-Prot : SWS_FT_FI7 34) chain A residue 330 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI8 35) 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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