eF-site ID 1xfu-O PDB Code 1xfu Chain O click to enlarge Title Crystal structure of anthrax edema factor (EF) truncation mutant, EF-delta 64 in complex with calmodulin Classification LYASE/Metal binding protein Compound Calmodulin-sensitive adenylate cyclase Source Bacillus anthracis (CALM_HUMAN) Sequence O:  QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQN PTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSE EEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVD QMIREADIDGDGQVNYEEFVQMMTAK Description Functional site 1) chain O residue 20 type sequence D description BINDING SITE FOR RESIDUE CA O 701 source : AC7 2) chain O residue 22 type sequence D description BINDING SITE FOR RESIDUE CA O 701 source : AC7 3) chain O residue 24 type sequence D description BINDING SITE FOR RESIDUE CA O 701 source : AC7 4) chain O residue 26 type sequence T description BINDING SITE FOR RESIDUE CA O 701 source : AC7 5) chain O residue 129 type sequence D description BINDING SITE FOR RESIDUE CA O 801 source : AC8 6) chain O residue 131 type sequence D description BINDING SITE FOR RESIDUE CA O 801 source : AC8 7) chain O residue 133 type sequence D description BINDING SITE FOR RESIDUE CA O 801 source : AC8 8) chain O residue 135 type sequence Q description BINDING SITE FOR RESIDUE CA O 801 source : AC8 9) chain O residue 140 type sequence E description BINDING SITE FOR RESIDUE CA O 801 source : AC8 10) chain O residue 93 type sequence D description BINDING SITE FOR RESIDUE CA O 802 source : AC9 11) chain O residue 95 type sequence D description BINDING SITE FOR RESIDUE CA O 802 source : AC9 12) chain O residue 97 type sequence N description BINDING SITE FOR RESIDUE CA O 802 source : AC9 13) chain O residue 99 type sequence Y description BINDING SITE FOR RESIDUE CA O 802 source : AC9 14) chain O residue 104 type sequence E description BINDING SITE FOR RESIDUE CA O 802 source : AC9 15) chain O residue 20-32 type prosite sequence DKDGDGTITTKEL description EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL source prosite : PS00018 16) chain O residue 56-68 type prosite sequence DADGNGTIDFPEF description EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL source prosite : PS00018 17) chain O residue 93-105 type prosite sequence DKDGNGYISAAEL description EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL source prosite : PS00018 18) chain O residue 129-141 type prosite sequence DIDGDGQVNYEEF description EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL source prosite : PS00018 19) chain O residue 20 type BINDING sequence D 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 O residue 67 type BINDING sequence E 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 21) chain O residue 22 type BINDING sequence D 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 22) chain O residue 24 type BINDING sequence D 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 23) chain O residue 26 type BINDING sequence T 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 24) chain O residue 31 type BINDING sequence E 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 25) chain O residue 56 type BINDING sequence D 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 26) chain O residue 58 type BINDING sequence D 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 27) chain O residue 60 type BINDING sequence N 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 28) chain O residue 62 type BINDING sequence T 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 29) chain O residue 110 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI10 30) chain O residue 115 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0007744|PubMed:24129315 source Swiss-Prot : SWS_FT_FI11 31) chain O residue 138 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI12 32) chain O 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 33) chain O 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 34) chain O 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 35) chain O 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 36) chain O 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 37) chain O 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 38) chain O 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 39) chain O 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 40) chain O 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 41) chain O 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 42) chain O 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 43) chain O residue 21 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 44) chain O residue 44 type MOD_RES sequence T description Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29 source Swiss-Prot : SWS_FT_FI5 45) chain O residue 81 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 46) chain O residue 94 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 47) chain O residue 99 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI8 48) chain O 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

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