eF-site ID 2hf5_10-A PDB Code 2hf5 Model 10 Chain A click to enlarge Title The structure and function of a novel two-site calcium-binding fragment of calmodulin Classification METAL BINDING PROTEIN Compound Calmodulin Source Homo sapiens (Human) (CALM_HUMAN) Sequence A:  AELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEI REAFRVFDKDGNGYISAAELRHVMTNLG Description Functional site 1) chain A residue 58 type sequence D description BINDING SITE FOR RESIDUE CA A 200 source : AC1 2) chain A residue 60 type sequence N description BINDING SITE FOR RESIDUE CA A 200 source : AC1 3) chain A residue 62 type sequence T description BINDING SITE FOR RESIDUE CA A 200 source : AC1 4) chain A residue 67 type sequence E description BINDING SITE FOR RESIDUE CA A 200 source : AC1 5) chain A residue 93 type sequence D description BINDING SITE FOR RESIDUE CA A 300 source : AC2 6) chain A residue 95 type sequence D description BINDING SITE FOR RESIDUE CA A 300 source : AC2 7) chain A residue 97 type sequence N description BINDING SITE FOR RESIDUE CA A 300 source : AC2 8) chain A residue 104 type sequence E description BINDING SITE FOR RESIDUE CA A 300 source : AC2 9) chain A residue 56-68 type prosite sequence DADGNGTIDFPEF description EF_HAND_1 EF-hand calcium-binding domain. DADGNGTIDfpEF source prosite : PS00018 10) chain A residue 93-105 type prosite sequence DKDGNGYISAAEL description EF_HAND_1 EF-hand calcium-binding domain. DADGNGTIDfpEF source prosite : PS00018 11) chain A residue 82 type MOD_RES sequence E description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 12) chain A residue 95 type MOD_RES sequence D description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 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_FI5 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_FI6 15) chain A residue 57 type BINDING sequence A description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 59 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 61 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 63 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 19) chain A residue 68 type BINDING sequence F description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 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_FI2 21) 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_FI2 22) 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_FI2 23) 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_FI2 24) 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_FI2 25) chain A residue 111 type MOD_RES sequence N description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7

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