eF-site ID 1stc-EI PDB Code 1stc Chain E, I click to enlarge Title CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC SUBUNIT IN COMPLEX WITH STAUROSPORINE Classification COMPLEX (TRANSFERASE/INHIBITOR) Compound CAMP-DEPENDENT PROTEIN KINASE Source Bos taurus (Bovine) (IPKA_HUMANX) Sequence E:  VKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGSF GRVMLVKHMETGNHYAMKILDKQKVVKLKQIEHTLNEKRI LQAVNFPFLVKLEFSFKDNSNLYMVMEYVPGGEMFSHLRR IGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLI DQQGYIQVTDFGFAKRVKGRTWXLCGTPEYLAPEIILSKG YNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGK VRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNH KWFATTDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEE IRVXINEKCGKEFSEF I:  TTYADFIASGRTGRRNA Description Functional site 1) chain E residue 49 type sequence L description BINDING SITE FOR RESIDUE STU E 351 source : AC1 2) chain E residue 50 type sequence G description BINDING SITE FOR RESIDUE STU E 351 source : AC1 3) chain E residue 57 type sequence V description BINDING SITE FOR RESIDUE STU E 351 source : AC1 4) chain E residue 70 type sequence A description BINDING SITE FOR RESIDUE STU E 351 source : AC1 5) chain E residue 72 type sequence K description BINDING SITE FOR RESIDUE STU E 351 source : AC1 6) chain E residue 120 type sequence M description BINDING SITE FOR RESIDUE STU E 351 source : AC1 7) chain E residue 121 type sequence E description BINDING SITE FOR RESIDUE STU E 351 source : AC1 8) chain E residue 122 type sequence Y description BINDING SITE FOR RESIDUE STU E 351 source : AC1 9) chain E residue 123 type sequence V description BINDING SITE FOR RESIDUE STU E 351 source : AC1 10) chain E residue 127 type sequence E description BINDING SITE FOR RESIDUE STU E 351 source : AC1 11) chain E residue 170 type sequence E description BINDING SITE FOR RESIDUE STU E 351 source : AC1 12) chain E residue 171 type sequence N description BINDING SITE FOR RESIDUE STU E 351 source : AC1 13) chain E residue 173 type sequence L description BINDING SITE FOR RESIDUE STU E 351 source : AC1 14) chain E residue 183 type sequence T description BINDING SITE FOR RESIDUE STU E 351 source : AC1 15) chain E residue 184 type sequence D description BINDING SITE FOR RESIDUE STU E 351 source : AC1 16) chain E residue 327 type sequence F description BINDING SITE FOR RESIDUE STU E 351 source : AC1 17) chain E residue 167 type catalytic sequence L description 757 source MCSA : MCSA1 18) chain E residue 169 type catalytic sequence P description 757 source MCSA : MCSA1 19) chain E residue 172 type catalytic sequence L description 757 source MCSA : MCSA1 20) chain E residue 185 type catalytic sequence F description 757 source MCSA : MCSA1 21) chain E residue 202 type catalytic sequence P description 757 source MCSA : MCSA1 22) chain E residue 50 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 23) chain E residue 73 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI2 24) chain E residue 122 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI3 25) chain E residue 169 type BINDING sequence P description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI3 26) chain I residue 16 type SITE sequence T description Important for inhibition source Swiss-Prot : SWS_FT_FI1 27) chain I residue 19 type SITE sequence R description Important for inhibition source Swiss-Prot : SWS_FT_FI1 28) chain I residue 20 type SITE sequence N description Important for inhibition source Swiss-Prot : SWS_FT_FI1 29) chain E residue 49 type MOD_RES sequence L description Phosphothreonine => ECO:0000250|UniProtKB:P17612 source Swiss-Prot : SWS_FT_FI6 30) chain E residue 196 type MOD_RES sequence W description Phosphothreonine => ECO:0000250|UniProtKB:P17612 source Swiss-Prot : SWS_FT_FI6 31) chain E residue 140 type MOD_RES sequence E description Phosphoserine => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI7 32) chain E residue 198 type MOD_RES sequence L description Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:6262777 source Swiss-Prot : SWS_FT_FI8 33) chain E residue 331 type MOD_RES sequence E description Phosphotyrosine => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI9 34) chain E residue 49-72 type prosite sequence LGTGSFGRVMLVKHMETGNHYAMK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGSFGRVMlVkhmetgnh..........YAMK source prosite : PS00107 35) chain E residue 162-174 type prosite sequence LIYRDLKPENLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiYrDLKpeNLLI source prosite : PS00108 36) 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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