eF-site ID 1a25-A PDB Code 1a25 Chain A click to enlarge Title C2 DOMAIN FROM PROTEIN KINASE C (BETA) Classification CALCIUM-BINDING PROTEIN Compound PROTEIN KINASE C (BETA) Source Rattus norvegicus (Rat) (KPCB_RAT) Sequence A:  ERRGRIYIQAHIDREVLIVVVRDAKNLVPMDPNGLSDPYV KLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDK DRRLSVEIWDWDLTSRNDFMGSLSFGISELQKAGVDGWFK LLSQEEGEYFNV Description Functional site 1) chain A residue 186 type sequence M description CA BINDING SITE. source : CLB 2) chain A residue 187 type sequence D description CA BINDING SITE. source : CLB 3) chain A residue 193 type sequence D description CA BINDING SITE. source : CLB 4) chain A residue 247 type sequence W description CA BINDING SITE. source : CLB 5) chain A residue 246 type sequence D description CA BINDING SITE. source : CLB 6) chain A residue 248 type sequence D description CA BINDING SITE. source : CLB 7) chain A residue 253 type sequence N description CA BINDING SITE. source : CLB 8) chain A residue 254 type sequence D description CA BINDING SITE. source : CLB 9) chain A residue 187 type sequence D description BINDING SITE FOR RESIDUE CA A 290 source : AC1 10) chain A residue 193 type sequence D description BINDING SITE FOR RESIDUE CA A 290 source : AC1 11) chain A residue 246 type sequence D description BINDING SITE FOR RESIDUE CA A 290 source : AC1 12) chain A residue 247 type sequence W description BINDING SITE FOR RESIDUE CA A 290 source : AC1 13) chain A residue 248 type sequence D description BINDING SITE FOR RESIDUE CA A 290 source : AC1 14) chain A residue 186 type sequence M description BINDING SITE FOR RESIDUE CA A 291 source : AC2 15) chain A residue 187 type sequence D description BINDING SITE FOR RESIDUE CA A 291 source : AC2 16) chain A residue 246 type sequence D description BINDING SITE FOR RESIDUE CA A 291 source : AC2 17) chain A residue 248 type sequence D description BINDING SITE FOR RESIDUE CA A 291 source : AC2 18) chain A residue 254 type sequence D description BINDING SITE FOR RESIDUE CA A 291 source : AC2 19) chain A residue 248 type sequence D description BINDING SITE FOR RESIDUE CA A 292 source : AC3 20) chain A residue 251 type sequence S description BINDING SITE FOR RESIDUE CA A 292 source : AC3 21) chain A residue 252 type sequence R description BINDING SITE FOR RESIDUE CA A 292 source : AC3 22) chain A residue 254 type sequence D description BINDING SITE FOR RESIDUE CA A 292 source : AC3 23) chain A residue 281 type sequence E description BINDING SITE FOR RESIDUE CA B 291 source : AC5 24) chain A residue 281 type sequence E description BINDING SITE FOR RESIDUE CA B 292 source : AC6 25) chain A residue 186 type BINDING sequence M description BINDING => ECO:0000269|PubMed:21215369, ECO:0000269|PubMed:9817842 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 187 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21215369, ECO:0000269|PubMed:9817842 source Swiss-Prot : SWS_FT_FI1 27) chain A residue 193 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21215369, ECO:0000269|PubMed:9817842 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 246 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21215369, ECO:0000269|PubMed:9817842 source Swiss-Prot : SWS_FT_FI1 29) chain A residue 247 type BINDING sequence W description BINDING => ECO:0000269|PubMed:21215369, ECO:0000269|PubMed:9817842 source Swiss-Prot : SWS_FT_FI1 30) chain A residue 248 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21215369, ECO:0000269|PubMed:9817842 source Swiss-Prot : SWS_FT_FI1 31) chain A residue 251 type BINDING sequence S description BINDING => ECO:0000269|PubMed:21215369, ECO:0000269|PubMed:9817842 source Swiss-Prot : SWS_FT_FI1 32) chain A residue 252 type BINDING sequence R description BINDING => ECO:0000269|PubMed:21215369, ECO:0000269|PubMed:9817842 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 254 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21215369, ECO:0000269|PubMed:9817842 source Swiss-Prot : SWS_FT_FI1 34) chain A residue 206 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P05771 source Swiss-Prot : SWS_FT_FI2 35) chain A residue 250 type MOD_RES sequence T description Phosphothreonine; by autocatalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3

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