eF-site ID 3ewt-A PDB Code 3ewt Chain A click to enlarge Title Crystal Structure of calmodulin complexed with a peptide Classification CALCIUM BINDING PROTEIN Compound Calmodulin Source (TNR6_HUMAN) Sequence A:  ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLG QNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTD SEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEE VDEMIREADIDGDGQVNYEEFVQMM Description Functional site 1) chain A residue 20 type sequence D description BINDING SITE FOR RESIDUE CA A 601 source : AC1 2) chain A residue 22 type sequence D description BINDING SITE FOR RESIDUE CA A 601 source : AC1 3) chain A residue 24 type sequence D description BINDING SITE FOR RESIDUE CA A 601 source : AC1 4) chain A residue 26 type sequence T description BINDING SITE FOR RESIDUE CA A 601 source : AC1 5) chain A residue 31 type sequence E description BINDING SITE FOR RESIDUE CA A 601 source : AC1 6) chain A residue 56 type sequence D description BINDING SITE FOR RESIDUE CA A 602 source : AC2 7) chain A residue 58 type sequence D description BINDING SITE FOR RESIDUE CA A 602 source : AC2 8) chain A residue 60 type sequence N description BINDING SITE FOR RESIDUE CA A 602 source : AC2 9) chain A residue 62 type sequence T description BINDING SITE FOR RESIDUE CA A 602 source : AC2 10) chain A residue 67 type sequence E description BINDING SITE FOR RESIDUE CA A 602 source : AC2 11) chain A residue 93 type sequence D description BINDING SITE FOR RESIDUE CA A 603 source : AC3 12) chain A residue 95 type sequence D description BINDING SITE FOR RESIDUE CA A 603 source : AC3 13) chain A residue 97 type sequence N description BINDING SITE FOR RESIDUE CA A 603 source : AC3 14) chain A residue 99 type sequence Y description BINDING SITE FOR RESIDUE CA A 603 source : AC3 15) chain A residue 104 type sequence E description BINDING SITE FOR RESIDUE CA A 603 source : AC3 16) chain A residue 129 type sequence D description BINDING SITE FOR RESIDUE CA A 604 source : AC4 17) chain A residue 131 type sequence D description BINDING SITE FOR RESIDUE CA A 604 source : AC4 18) chain A residue 133 type sequence D description BINDING SITE FOR RESIDUE CA A 604 source : AC4 19) chain A residue 135 type sequence Q description BINDING SITE FOR RESIDUE CA A 604 source : AC4 20) chain A residue 140 type sequence E description BINDING SITE FOR RESIDUE CA A 604 source : AC4 21) chain A residue 110 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI10 22) chain A residue 67 type CARBOHYD sequence E description (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:30979585, ECO:0000305|PubMed:23955153 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 22 type CARBOHYD sequence D description (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:30979585, ECO:0000305|PubMed:23955153 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 24 type CARBOHYD sequence D description (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:30979585, ECO:0000305|PubMed:23955153 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 26 type CARBOHYD sequence T description (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:30979585, ECO:0000305|PubMed:23955153 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 31 type CARBOHYD sequence E description (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:30979585, ECO:0000305|PubMed:23955153 source Swiss-Prot : SWS_FT_FI1 27) chain A residue 56 type CARBOHYD sequence D description (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:30979585, ECO:0000305|PubMed:23955153 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 58 type CARBOHYD sequence D description (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:30979585, ECO:0000305|PubMed:23955153 source Swiss-Prot : SWS_FT_FI1 29) chain A residue 60 type CARBOHYD sequence N description (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:30979585, ECO:0000305|PubMed:23955153 source Swiss-Prot : SWS_FT_FI1 30) chain A residue 62 type CARBOHYD sequence T description (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:30979585, ECO:0000305|PubMed:23955153 source Swiss-Prot : SWS_FT_FI1 31) chain A residue 99 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI8 32) chain A residue 115 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0007744|PubMed:24129315 source Swiss-Prot : SWS_FT_FI11 33) chain A residue 138 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI12 34) chain A residue 21 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157 source Swiss-Prot : SWS_FT_FI13 35) chain A residue 21 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 36) chain A residue 44 type MOD_RES sequence T description Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29 source Swiss-Prot : SWS_FT_FI5 37) chain A residue 81 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 38) chain A residue 94 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 39) chain A residue 101 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 40) chain A residue 20-32 type prosite sequence DKDGDGTITTKEL description EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL source prosite : PS00018 41) chain A residue 56-68 type prosite sequence DADGNGTIDFPEF description EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL source prosite : PS00018 42) chain A residue 93-105 type prosite sequence DKDGNGYISAAEL description EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL source prosite : PS00018 43) chain A residue 129-141 type prosite sequence DIDGDGQVNYEEF description EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL source prosite : PS00018 44) chain A residue 93 type BINDING sequence D 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_FI2 45) chain A residue 140 type BINDING sequence E 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_FI2 46) chain A residue 95 type BINDING sequence D 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_FI2 47) chain A residue 97 type BINDING sequence N 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_FI2 48) chain A residue 99 type BINDING sequence Y 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_FI2 49) chain A residue 104 type BINDING sequence E 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_FI2 50) chain A residue 129 type BINDING sequence D 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_FI2 51) chain A residue 131 type BINDING sequence D 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_FI2 52) chain A residue 133 type BINDING sequence D 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_FI2 53) chain A residue 135 type BINDING sequence Q 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_FI2 54) chain A residue 1 type MOD_RES sequence A description N-acetylalanine => ECO:0000269|PubMed:7093203, ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI3

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