eF-site ID 4iak-AS PDB Code 4iak Chain A, S click to enlarge Title Low temperature X-ray structure of cAMP dependent protein kinase A in complex with high Sr2+ concentration, ADP and phosphorylated peptide pSP20 Classification Transferase/Peptide Compound cAMP-dependent protein kinase catalytic subunit alpha Source Mus musculus (Mouse) (4IAK) Sequence A:  SVKEFLAKAKEDFLKKWETPSQNTAQLDQFDRIKTLGTGS FGRVMLVKHKESGNHYAMKILDKQKVVKLKQIEHTLNEKR ILQAVNFPFLVKLEFSFKDNSNLYMVMEYVAGGEMFSHLR RIGRFXEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLL IDQQGYIQVTDFGFAKRVKGRTWXLCGTPEYLAPEIILSK GYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSG KVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKN HKWFATTDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEE EIRVXINEKCGKEFTEF S:  TTYADFIASGRTGRRAXIHD Description (1)  cAMP-dependent protein kinase catalytic subunit alpha (E.C.2.7.11.11), phosphorylated pseudo-substrate peptide pSP20 Functional site 1) chain A residue 184 type sequence D description BINDING SITE FOR RESIDUE SR A 401 source : AC1 2) chain S residue 621 type sequence X description BINDING SITE FOR RESIDUE SR A 401 source : AC1 3) chain A residue 171 type sequence N description BINDING SITE FOR RESIDUE SR A 402 source : AC2 4) chain A residue 184 type sequence D description BINDING SITE FOR RESIDUE SR A 402 source : AC2 5) chain A residue 49 type sequence L description BINDING SITE FOR RESIDUE ADP A 403 source : AC3 6) chain A residue 52 type sequence G description BINDING SITE FOR RESIDUE ADP A 403 source : AC3 7) chain A residue 53 type sequence S description BINDING SITE FOR RESIDUE ADP A 403 source : AC3 8) chain A residue 57 type sequence V description BINDING SITE FOR RESIDUE ADP A 403 source : AC3 9) chain A residue 70 type sequence A description BINDING SITE FOR RESIDUE ADP A 403 source : AC3 10) chain A residue 72 type sequence K description BINDING SITE FOR RESIDUE ADP A 403 source : AC3 11) chain A residue 104 type sequence V description BINDING SITE FOR RESIDUE ADP A 403 source : AC3 12) chain A residue 120 type sequence M description BINDING SITE FOR RESIDUE ADP A 403 source : AC3 13) chain A residue 121 type sequence E description BINDING SITE FOR RESIDUE ADP A 403 source : AC3 14) chain A residue 122 type sequence Y description BINDING SITE FOR RESIDUE ADP A 403 source : AC3 15) chain A residue 123 type sequence V description BINDING SITE FOR RESIDUE ADP A 403 source : AC3 16) chain A residue 127 type sequence E description BINDING SITE FOR RESIDUE ADP A 403 source : AC3 17) chain A residue 170 type sequence E description BINDING SITE FOR RESIDUE ADP A 403 source : AC3 18) chain A residue 171 type sequence N description BINDING SITE FOR RESIDUE ADP A 403 source : AC3 19) chain A residue 173 type sequence L description BINDING SITE FOR RESIDUE ADP A 403 source : AC3 20) chain A residue 183 type sequence T description BINDING SITE FOR RESIDUE ADP A 403 source : AC3 21) chain A residue 184 type sequence D description BINDING SITE FOR RESIDUE ADP A 403 source : AC3 22) chain A residue 327 type sequence F description BINDING SITE FOR RESIDUE ADP A 403 source : AC3 23) chain S residue 618 type sequence R description BINDING SITE FOR RESIDUE ADP A 403 source : AC3 24) chain S residue 621 type sequence X description BINDING SITE FOR RESIDUE ADP A 403 source : AC3 25) chain A residue 64 type sequence E description BINDING SITE FOR RESIDUE CO3 A 404 source : AC4 26) chain A residue 83 type sequence K description BINDING SITE FOR RESIDUE CO3 A 404 source : AC4 27) chain A residue 85 type sequence I description BINDING SITE FOR RESIDUE CO3 A 404 source : AC4 28) chain A residue 86 type sequence E description BINDING SITE FOR RESIDUE CO3 A 404 source : AC4 29) chain A residue 48 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P17612 source Swiss-Prot : SWS_FT_FI5 30) chain A residue 195 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P17612 source Swiss-Prot : SWS_FT_FI5 31) chain A residue 139 type MOD_RES sequence X description Phosphoserine => ECO:0000269|PubMed:22323819, ECO:0000305|PubMed:8395513 source Swiss-Prot : SWS_FT_FI6 32) chain A residue 197 type MOD_RES sequence X description Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:22323819, ECO:0000269|PubMed:8395513, ECO:0000269|PubMed:9707564 source Swiss-Prot : SWS_FT_FI7 33) chain A residue 330 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:21866565 source Swiss-Prot : SWS_FT_FI8 34) chain A residue 338 type MOD_RES sequence X description Phosphoserine => ECO:0000305|PubMed:8395513 source Swiss-Prot : SWS_FT_FI9 35) chain S residue 615 type SITE sequence R description Important for inhibition => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 36) chain S residue 618 type SITE sequence R description Important for inhibition => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 37) chain S residue 619 type SITE sequence R description Important for inhibition => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 38) chain A residue 49 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 39) chain A residue 72 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 40) chain A residue 121 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 41) chain A residue 168 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 42) chain A residue 49-72 type prosite sequence LGTGSFGRVMLVKHKESGNHYAMK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGSFGRVMlVkhkesgnh..........YAMK source prosite : PS00107 43) chain A residue 162-174 type prosite sequence LIYRDLKPENLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiYrDLKpeNLLI source prosite : PS00108

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