eF-site ID 1yrt-B PDB Code 1yrt Chain B click to enlarge Title Crystal Structure analysis of the adenylyl cyclaes catalytic domain of adenylyl cyclase toxin of Bordetella pertussis in presence of c-terminal calmodulin Classification LAYSE, TOXIN Compound Bifunctional hemolysin-adenylate cyclase Source null (CALM_HUMAN) Sequence B:  TDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTD EEVDEMIREADIDGDGQVNYEEFVQMMTA Description Functional site 1) chain B residue 129 type sequence D description BINDING SITE FOR RESIDUE CA B 800 source : AC1 2) chain B residue 131 type sequence D description BINDING SITE FOR RESIDUE CA B 800 source : AC1 3) chain B residue 133 type sequence D description BINDING SITE FOR RESIDUE CA B 800 source : AC1 4) chain B residue 135 type sequence Q description BINDING SITE FOR RESIDUE CA B 800 source : AC1 5) chain B residue 140 type sequence E description BINDING SITE FOR RESIDUE CA B 800 source : AC1 6) chain B residue 93 type sequence D description BINDING SITE FOR RESIDUE CA B 801 source : AC2 7) chain B residue 95 type sequence D description BINDING SITE FOR RESIDUE CA B 801 source : AC2 8) chain B residue 97 type sequence N description BINDING SITE FOR RESIDUE CA B 801 source : AC2 9) chain B residue 99 type sequence Y description BINDING SITE FOR RESIDUE CA B 801 source : AC2 10) chain B residue 104 type sequence E description BINDING SITE FOR RESIDUE CA B 801 source : AC2 11) chain B residue 93-105 type prosite sequence DKDGNGYISAAEL description EF_HAND_1 EF-hand calcium-binding domain. DKDGNGYISaaEL source prosite : PS00018 12) chain B residue 129-141 type prosite sequence DIDGDGQVNYEEF description EF_HAND_1 EF-hand calcium-binding domain. DKDGNGYISaaEL source prosite : PS00018 13) chain B residue 82 type MOD_RES sequence E description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 14) chain B residue 95 type MOD_RES sequence D description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 15) chain B residue 100 type MOD_RES sequence I description Phosphotyrosine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI4 16) chain B 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 17) chain B 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 18) chain B 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 19) chain B 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 20) chain B 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 B 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 B 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 23) chain B 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 24) chain B 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 25) chain B 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 26) chain B 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 27) chain B residue 111 type MOD_RES sequence N description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 28) chain B residue 116 type MOD_RES sequence L description N6-methyllysine; alternate => ECO:0007744|PubMed:24129315 source Swiss-Prot : SWS_FT_FI7 29) chain B residue 139 type MOD_RES sequence E description Phosphotyrosine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI8

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