eF-site ID 1j7p_3-A PDB Code 1j7p Model 3 Chain A click to enlarge Title Solution structure of Calcium calmodulin C-terminal domain Classification METAL BINDING PROTEIN Compound Calmodulin Source Homo sapiens (Human) (CALM_HUMAN) Sequence A:  EEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEV DEMIREADIDGDGQVNYEEFVQMMTAK Description Functional site 1) chain A residue 93 type sequence D description BINDING SITE FOR RESIDUE CA A 1000 source : AC1 2) chain A residue 95 type sequence D description BINDING SITE FOR RESIDUE CA A 1000 source : AC1 3) chain A residue 97 type sequence N description BINDING SITE FOR RESIDUE CA A 1000 source : AC1 4) chain A residue 99 type sequence Y description BINDING SITE FOR RESIDUE CA A 1000 source : AC1 5) chain A residue 104 type sequence E description BINDING SITE FOR RESIDUE CA A 1000 source : AC1 6) chain A residue 129 type sequence D description BINDING SITE FOR RESIDUE CA A 1001 source : AC2 7) chain A residue 131 type sequence D description BINDING SITE FOR RESIDUE CA A 1001 source : AC2 8) chain A residue 133 type sequence D description BINDING SITE FOR RESIDUE CA A 1001 source : AC2 9) chain A residue 135 type sequence Q description BINDING SITE FOR RESIDUE CA A 1001 source : AC2 10) chain A residue 137 type sequence N description BINDING SITE FOR RESIDUE CA A 1001 source : AC2 11) chain A residue 140 type sequence E description BINDING SITE FOR RESIDUE CA A 1001 source : AC2 12) chain A residue 95 type MOD_RES sequence D description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 13) chain A residue 100 type MOD_RES sequence I description Phosphotyrosine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI4 14) chain A residue 102 type MOD_RES sequence A description Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5 15) chain A residue 111 type MOD_RES sequence N description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 16) chain A residue 116 type MOD_RES sequence L description N6-methyllysine; alternate => ECO:0007744|PubMed:24129315 source Swiss-Prot : SWS_FT_FI7 17) chain A residue 139 type MOD_RES sequence E description Phosphotyrosine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI8 18) chain A residue 93-105 type prosite sequence DKDGNGYISAAEL description EF_HAND_1 EF-hand calcium-binding domain. DKDGNGYISaaEL source prosite : PS00018 19) chain A residue 129-141 type prosite sequence DIDGDGQVNYEEF description EF_HAND_1 EF-hand calcium-binding domain. DKDGNGYISaaEL source prosite : PS00018 20) chain A residue 94 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 141 type BINDING sequence F description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 96 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 98 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 100 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 105 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 130 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 27) chain A residue 132 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 134 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 29) chain A residue 136 type BINDING sequence V description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 30) chain A residue 82 type MOD_RES sequence E description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2

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