eF-site ID 1xfu-R PDB Code 1xfu Chain R 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 R:  QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQN PTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSE EEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVD QMIREADIDGDGQVNYEEFVQMMTAK Description Functional site 1) chain R residue 20 type sequence D description BINDING SITE FOR RESIDUE CA R 707 source : BC7 2) chain R residue 22 type sequence D description BINDING SITE FOR RESIDUE CA R 707 source : BC7 3) chain R residue 24 type sequence D description BINDING SITE FOR RESIDUE CA R 707 source : BC7 4) chain R residue 26 type sequence T description BINDING SITE FOR RESIDUE CA R 707 source : BC7 5) chain R residue 129 type sequence D description BINDING SITE FOR RESIDUE CA R 807 source : BC8 6) chain R residue 131 type sequence D description BINDING SITE FOR RESIDUE CA R 807 source : BC8 7) chain R residue 133 type sequence D description BINDING SITE FOR RESIDUE CA R 807 source : BC8 8) chain R residue 135 type sequence Q description BINDING SITE FOR RESIDUE CA R 807 source : BC8 9) chain R residue 140 type sequence E description BINDING SITE FOR RESIDUE CA R 807 source : BC8 10) chain R residue 93 type sequence D description BINDING SITE FOR RESIDUE CA R 808 source : BC9 11) chain R residue 95 type sequence D description BINDING SITE FOR RESIDUE CA R 808 source : BC9 12) chain R residue 97 type sequence N description BINDING SITE FOR RESIDUE CA R 808 source : BC9 13) chain R residue 99 type sequence Y description BINDING SITE FOR RESIDUE CA R 808 source : BC9 14) chain R residue 104 type sequence E description BINDING SITE FOR RESIDUE CA R 808 source : BC9 15) chain R residue 110 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI10 16) chain R residue 115 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0007744|PubMed:24129315 source Swiss-Prot : SWS_FT_FI11 17) chain R residue 138 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI12 18) chain R 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 19) chain R 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 20) chain R 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 21) chain R 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 22) chain R 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 23) chain R 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 24) chain R 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 25) chain R 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 26) chain R 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 27) chain R 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 28) chain R 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 29) chain R residue 81 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 30) chain R 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 31) chain R 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 32) chain R 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 33) chain R 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 34) chain R 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 35) chain R 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 36) chain R 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 37) chain R 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 38) chain R 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 39) chain R 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 40) chain R 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 41) chain R residue 21 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 42) chain R residue 44 type MOD_RES sequence T description Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29 source Swiss-Prot : SWS_FT_FI5 43) chain R residue 94 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 44) chain R residue 99 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI8

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