eF-site ID 3if7-A PDB Code 3if7 Chain A click to enlarge Title Structure of Calmodulin complexed with its first endogenous inhibitor, sphingosylphosphorylcholine Classification CALCIUM BINDING PROTEIN Compound Calmodulin Source ORGANISM_COMMON: Bovine; ORGANISM_SCIENTIFIC: Bos taurus; Sequence A:  QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQN PTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDSEEE IREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEM IREADIDGDGQVNYEEFVQMMT Description Functional site 1) chain A residue 20 type sequence D description BINDING SITE FOR RESIDUE CA A 149 source : AC1 2) chain A residue 22 type sequence D description BINDING SITE FOR RESIDUE CA A 149 source : AC1 3) chain A residue 24 type sequence D description BINDING SITE FOR RESIDUE CA A 149 source : AC1 4) chain A residue 26 type sequence T description BINDING SITE FOR RESIDUE CA A 149 source : AC1 5) chain A residue 31 type sequence E description BINDING SITE FOR RESIDUE CA A 149 source : AC1 6) chain A residue 56 type sequence D description BINDING SITE FOR RESIDUE CA A 150 source : AC2 7) chain A residue 58 type sequence D description BINDING SITE FOR RESIDUE CA A 150 source : AC2 8) chain A residue 60 type sequence N description BINDING SITE FOR RESIDUE CA A 150 source : AC2 9) chain A residue 62 type sequence T description BINDING SITE FOR RESIDUE CA A 150 source : AC2 10) chain A residue 67 type sequence E description BINDING SITE FOR RESIDUE CA A 150 source : AC2 11) chain A residue 93 type sequence D description BINDING SITE FOR RESIDUE CA A 151 source : AC3 12) chain A residue 95 type sequence D description BINDING SITE FOR RESIDUE CA A 151 source : AC3 13) chain A residue 97 type sequence N description BINDING SITE FOR RESIDUE CA A 151 source : AC3 14) chain A residue 99 type sequence Y description BINDING SITE FOR RESIDUE CA A 151 source : AC3 15) chain A residue 104 type sequence E description BINDING SITE FOR RESIDUE CA A 151 source : AC3 16) chain A residue 129 type sequence D description BINDING SITE FOR RESIDUE CA A 152 source : AC4 17) chain A residue 131 type sequence D description BINDING SITE FOR RESIDUE CA A 152 source : AC4 18) chain A residue 133 type sequence D description BINDING SITE FOR RESIDUE CA A 152 source : AC4 19) chain A residue 135 type sequence Q description BINDING SITE FOR RESIDUE CA A 152 source : AC4 20) chain A residue 140 type sequence E description BINDING SITE FOR RESIDUE CA A 152 source : AC4 21) chain A residue 11 type sequence E description BINDING SITE FOR RESIDUE SPU A 153 source : AC5 22) chain A residue 76 type sequence M description BINDING SITE FOR RESIDUE SPU A 153 source : AC5 23) chain A residue 88 type sequence A description BINDING SITE FOR RESIDUE SPU A 153 source : AC5 24) chain A residue 92 type sequence F description BINDING SITE FOR RESIDUE SPU A 153 source : AC5 25) chain A residue 123 type sequence E description BINDING SITE FOR RESIDUE SPU A 153 source : AC5 26) chain A residue 124 type sequence M description BINDING SITE FOR RESIDUE SPU A 153 source : AC5 27) chain A residue 127 type sequence E description BINDING SITE FOR RESIDUE SPU A 153 source : AC5 28) chain A residue 141 type sequence F description BINDING SITE FOR RESIDUE SPU A 153 source : AC5 29) chain A residue 144 type sequence M description BINDING SITE FOR RESIDUE SPU A 153 source : AC5 30) chain A residue 145 type sequence M description BINDING SITE FOR RESIDUE SPU A 153 source : AC5 31) chain A residue 11 type sequence E description BINDING SITE FOR RESIDUE SPU A 154 source : AC6 32) chain A residue 39 type sequence L description BINDING SITE FOR RESIDUE SPU A 154 source : AC6 33) chain A residue 87 type sequence E description BINDING SITE FOR RESIDUE SPU A 154 source : AC6 34) chain A residue 124 type sequence M description BINDING SITE FOR RESIDUE SPU A 154 source : AC6 35) chain A residue 12 type sequence F description BINDING SITE FOR RESIDUE SPU A 155 source : AC7 36) chain A residue 15 type sequence A description BINDING SITE FOR RESIDUE SPU A 155 source : AC7 37) chain A residue 32 type sequence L description BINDING SITE FOR RESIDUE SPU A 155 source : AC7 38) chain A residue 51 type sequence M description BINDING SITE FOR RESIDUE SPU A 155 source : AC7 39) chain A residue 54 type sequence E description BINDING SITE FOR RESIDUE SPU A 155 source : AC7 40) chain A residue 55 type sequence V description BINDING SITE FOR RESIDUE SPU A 155 source : AC7 41) chain A residue 71 type sequence M description BINDING SITE FOR RESIDUE SPU A 155 source : AC7 42) chain A residue 72 type sequence M description BINDING SITE FOR RESIDUE SPU A 155 source : AC7 43) chain A residue 145 type sequence M description BINDING SITE FOR RESIDUE SPU A 156 source : AC8 44) chain A residue 20-32 type prosite sequence DKDGDGTITTKEL description EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL source prosite : PS00018 45) chain A residue 56-68 type prosite sequence DADGNGTIDFPEF description EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL source prosite : PS00018 46) chain A residue 93-105 type prosite sequence DKDGNGYISAAEL description EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL source prosite : PS00018 47) chain A residue 129-141 type prosite sequence DIDGDGQVNYEEF description EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL source prosite : PS00018 48) chain A residue 101 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P0DP23 source Swiss-Prot : SWS_FT_FI5 49) chain A residue 81 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P0DP23 source Swiss-Prot : SWS_FT_FI5 50) chain A residue 94 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P0DP23 source Swiss-Prot : SWS_FT_FI6 51) chain A residue 138 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P0DP23 source Swiss-Prot : SWS_FT_FI7 52) chain A residue 99 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P0DP23 source Swiss-Prot : SWS_FT_FI7 53) chain A residue 110 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P0DP23 source Swiss-Prot : SWS_FT_FI8 54) chain A residue 115 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000250|UniProtKB:P0DP23 source Swiss-Prot : SWS_FT_FI9 55) chain A residue 21 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:9716384 source Swiss-Prot : SWS_FT_FI10 56) chain A residue 67 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 57) chain A residue 93 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 58) chain A residue 95 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 59) chain A residue 97 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 60) chain A residue 99 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 61) chain A residue 104 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 62) chain A residue 129 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 63) chain A residue 131 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 64) chain A residue 133 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 65) chain A residue 135 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 66) chain A residue 140 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 67) chain A residue 56 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 68) chain A residue 58 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 69) chain A residue 60 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 70) chain A residue 62 type BINDING sequence T description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 71) chain A residue 20 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 72) chain A residue 22 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 73) chain A residue 24 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 74) chain A residue 26 type BINDING sequence T description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 75) chain A residue 31 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 76) chain A residue 21 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P0DP23 source Swiss-Prot : SWS_FT_FI3 77) chain A residue 44 type MOD_RES sequence T description Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29 source Swiss-Prot : SWS_FT_FI4

Display surface Download Links