eF-site ID 2f7z-E PDB Code 2f7z Chain E click to enlarge Title Protein Kinase A bound to (R)-1-(1H-Indol-3-ylmethyl)-2-(2-pyridin-4-yl-[1,7]naphtyridin-5-yloxy)-ehylamine Classification TRANSFERASE Compound cAMP-dependent protein kinase, alpha-catalytic subunit Source Bos taurus (Bovine) (2F7Z) Sequence E:  VKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGSF GRVMLVKHMETGNHYAMKILDKQKVVKLKQIEHTLNEKRI LQAVNFPFLVKLEFSFKDNSNLYMVMEYVPGGEMFSHLRR IGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI DQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKG YNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGK VRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNH KWFATTDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEE IRVSINEKCGKEFSEF Description Functional site 1) chain E residue 52 type sequence G description BINDING SITE FOR RESIDUE 6EA E 1000 source : AC1 2) chain E residue 53 type sequence S description BINDING SITE FOR RESIDUE 6EA E 1000 source : AC1 3) chain E residue 55 type sequence G description BINDING SITE FOR RESIDUE 6EA E 1000 source : AC1 4) chain E residue 70 type sequence A description BINDING SITE FOR RESIDUE 6EA E 1000 source : AC1 5) chain E residue 72 type sequence K description BINDING SITE FOR RESIDUE 6EA E 1000 source : AC1 6) chain E residue 121 type sequence E description BINDING SITE FOR RESIDUE 6EA E 1000 source : AC1 7) chain E residue 122 type sequence Y description BINDING SITE FOR RESIDUE 6EA E 1000 source : AC1 8) chain E residue 123 type sequence V description BINDING SITE FOR RESIDUE 6EA E 1000 source : AC1 9) chain E residue 168 type sequence K description BINDING SITE FOR RESIDUE 6EA E 1000 source : AC1 10) chain E residue 171 type sequence N description BINDING SITE FOR RESIDUE 6EA E 1000 source : AC1 11) chain E residue 173 type sequence L description BINDING SITE FOR RESIDUE 6EA E 1000 source : AC1 12) chain E residue 183 type sequence T description BINDING SITE FOR RESIDUE 6EA E 1000 source : AC1 13) chain E residue 184 type sequence D description BINDING SITE FOR RESIDUE 6EA E 1000 source : AC1 14) chain E residue 327 type sequence F description BINDING SITE FOR RESIDUE 6EA E 1000 source : AC1 15) chain E residue 167 type catalytic sequence L description 757 source MCSA : MCSA1 16) chain E residue 169 type catalytic sequence P description 757 source MCSA : MCSA1 17) chain E residue 172 type catalytic sequence L description 757 source MCSA : MCSA1 18) chain E residue 185 type catalytic sequence F description 757 source MCSA : MCSA1 19) chain E residue 202 type catalytic sequence P description 757 source MCSA : MCSA1 20) chain E residue 49 type MOD_RES sequence L description Phosphothreonine => ECO:0000250|UniProtKB:P17612 source Swiss-Prot : SWS_FT_FI6 21) chain E residue 196 type MOD_RES sequence W description Phosphothreonine => ECO:0000250|UniProtKB:P17612 source Swiss-Prot : SWS_FT_FI6 22) chain E residue 140 type MOD_RES sequence E description Phosphoserine => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI7 23) chain E residue 198 type MOD_RES sequence L description Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:6262777 source Swiss-Prot : SWS_FT_FI8 24) chain E residue 331 type MOD_RES sequence E description Phosphotyrosine => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI9 25) chain E residue 50 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 26) chain E residue 73 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI2 27) chain E residue 122 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI3 28) chain E residue 169 type BINDING sequence P description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI3 29) chain E residue 49-72 type prosite sequence LGTGSFGRVMLVKHMETGNHYAMK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGSFGRVMlVkhmetgnh..........YAMK source prosite : PS00107 30) chain E residue 162-174 type prosite sequence LIYRDLKPENLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiYrDLKpeNLLI source prosite : PS00108 31) chain E residue 339 type MOD_RES sequence I description Phosphoserine => ECO:0000269|PubMed:6262777 source Swiss-Prot : SWS_FT_FI10

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