eF-site ID 5vhb-AB PDB Code 5vhb Chain A, B click to enlarge Title Crystal structure of Protein Kinase A in complex with the PKI peptide and Aminobenzothiazole based inhibitor Classification TRANSFERASE Compound cAMP-dependent protein kinase catalytic subunit alpha Source Bos taurus (Bovine) (IPKA_BOVIN) Sequence A:  FLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGSFGRV MLVKHMETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQA VNFPFLVKLEFSFKDNSNLYMVMEYVPGGEMFSHLRRIGR FXEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQ GYIQVTDFGFAKRVKGRTWXLCGTPEYLAPEIILSKGYNK AVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRF PSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWF ATTDWIAIYQRKVEAPFIPGDTSNFDDYEEEEIRVXINEK CGKEFSEF B:  TTYADFIASGRTGRRNAI Description (1)  cAMP-dependent protein kinase catalytic subunit alpha (E.C.2.7.11.11), PKI peptide Functional site 1) chain A residue 53 type sequence G description binding site for residue 9CY A 401 source : AC1 2) chain A residue 56 type sequence G description binding site for residue 9CY A 401 source : AC1 3) chain A residue 57 type sequence R description binding site for residue 9CY A 401 source : AC1 4) chain A residue 58 type sequence V description binding site for residue 9CY A 401 source : AC1 5) chain A residue 71 type sequence A description binding site for residue 9CY A 401 source : AC1 6) chain A residue 73 type sequence K description binding site for residue 9CY A 401 source : AC1 7) chain A residue 122 type sequence E description binding site for residue 9CY A 401 source : AC1 8) chain A residue 123 type sequence Y description binding site for residue 9CY A 401 source : AC1 9) chain A residue 124 type sequence V description binding site for residue 9CY A 401 source : AC1 10) chain A residue 172 type sequence N description binding site for residue 9CY A 401 source : AC1 11) chain A residue 174 type sequence L description binding site for residue 9CY A 401 source : AC1 12) chain A residue 184 type sequence T description binding site for residue 9CY A 401 source : AC1 13) chain A residue 185 type sequence D description binding site for residue 9CY A 401 source : AC1 14) chain A residue 50-73 type prosite sequence LGTGSFGRVMLVKHMETGNHYAMK description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGSFGRVMlVkhmetgnh..........YAMK source prosite : PS00107 15) chain A residue 163-175 type prosite sequence LIYRDLKPENLLI description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiYrDLKpeNLLI source prosite : PS00108 16) chain A residue 167 type catalytic sequence D description 757 source MCSA : MCSA1 17) chain A residue 169 type catalytic sequence K description 757 source MCSA : MCSA1 18) chain A residue 172 type catalytic sequence N description 757 source MCSA : MCSA1 19) chain A residue 185 type catalytic sequence D description 757 source MCSA : MCSA1 20) chain A residue 202 type catalytic sequence T description 757 source MCSA : MCSA1 21) chain B residue 16 type SITE sequence R description Important for inhibition => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 22) chain B residue 17 type SITE sequence R description Important for inhibition => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 23) chain B residue 13 type SITE sequence R description Important for inhibition => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 73 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 25) chain A residue 50 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 26) chain A residue 169 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI3 27) chain A residue 122 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI3 28) chain A residue 49 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P17612 source Swiss-Prot : SWS_FT_FI6 29) chain A residue 196 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P17612 source Swiss-Prot : SWS_FT_FI6 30) chain A residue 140 type MOD_RES sequence X description Phosphoserine => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI7 31) chain A residue 198 type MOD_RES sequence X description Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:6262777 source Swiss-Prot : SWS_FT_FI8 32) chain A residue 331 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P05132 source Swiss-Prot : SWS_FT_FI9 33) chain A residue 339 type MOD_RES sequence X description Phosphoserine => ECO:0000269|PubMed:6262777 source Swiss-Prot : SWS_FT_FI10

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