eF-site ID 2col-B PDB Code 2col Chain B click to enlarge Title Crystal structure analysis of CyaA/C-Cam with Pyrophosphate Classification LYASE/METAL BINDING PROTEIN Compound Bifunctional hemolysin-adenylate cyclase Source Bordetella pertussis (CALM_XENLA) Sequence B:  TDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTD EEVDEMIREADIDGDGQVNYEEFVQMM 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 94 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 14) chain B residue 141 type BINDING sequence F description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 15) chain B residue 96 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 16) chain B residue 98 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 17) chain B residue 100 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 18) chain B residue 105 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 19) chain B residue 130 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 20) chain B residue 132 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 21) chain B residue 134 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 22) chain B residue 136 type BINDING sequence V description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 23) chain B residue 116 type MOD_RES sequence L description N6,N6,N6-trimethyllysine => ECO:0000250|UniProtKB:P0DP23 source Swiss-Prot : SWS_FT_FI2

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