eF-site ID 6oqq-D PDB Code 6oqq Chain D click to enlarge Title Legionella pneumophila SidJ/Saccharomyces cerevisiae calmodulin complex Classification TRANSFERASE Compound Legionella pneumophila SidJ Source (CALM_YEAST) Sequence D:  LTEEQIAEFKEAFALFDKDNNGSISSSELATVMRSLGLSP SEAEVNDLMNEIDVDGNHQIEFSEFLALMSRQLKSNDSEQ ELLEAFKVFDKNGDGLISAAELKHVLTSIGEKLTDAEVDD MNIQQFAALLS Description Functional site 1) chain D residue 21 type sequence D description binding site for residue CA D 201 source : AF3 2) chain D residue 23 type sequence D description binding site for residue CA D 201 source : AF3 3) chain D residue 25 type sequence N description binding site for residue CA D 201 source : AF3 4) chain D residue 27 type sequence S description binding site for residue CA D 201 source : AF3 5) chain D residue 94 type sequence D description binding site for residue CA D 202 source : AF4 6) chain D residue 96 type sequence N description binding site for residue CA D 202 source : AF4 7) chain D residue 98 type sequence D description binding site for residue CA D 202 source : AF4 8) chain D residue 100 type sequence L description binding site for residue CA D 202 source : AF4 9) chain D residue 21 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 10) chain D residue 23 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 11) chain D residue 25 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 12) chain D residue 27 type BINDING sequence S description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 13) chain D residue 32 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 14) chain D residue 57 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 15) chain D residue 59 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 16) chain D residue 61 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 17) chain D residue 63 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 18) chain D residue 68 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 19) chain D residue 94 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 20) chain D residue 96 type BINDING sequence N description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 21) chain D residue 98 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 22) chain D residue 105 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 source Swiss-Prot : SWS_FT_FI1 23) chain D residue 82 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI2 24) chain D residue 102 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI3

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