eF-site ID 5j31-A PDB Code 5j31 Chain A click to enlarge Title Crystal structure of 14-3-3zeta in complex with an alkyne cross-linked cyclic peptide derived from ExoS Classification SIGNALING PROTEIN Compound 14-3-3 protein zeta/delta Source Homo sapiens (Human) (Q93SQ3_PSEAI) Sequence A:  MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEE RNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAR EYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLK MKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEM QPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAI AELDTLEESYKDSTLIMQLLRDNLTLWTS Description Functional site 1) chain A residue 222 type sequence R description binding site for residue BEZ B 301 source : AC1 2) chain A residue 41 type sequence R description binding site for Di-peptide ASP C 424 and ZS8 C 425 source : AC2 3) chain A residue 42 type sequence N description binding site for Di-peptide ASP C 424 and ZS8 C 425 source : AC2 4) chain A residue 45 type sequence S description binding site for Di-peptide ASP C 424 and ZS8 C 425 source : AC2 5) chain A residue 49 type sequence K description binding site for Di-peptide ASP C 424 and ZS8 C 425 source : AC2 6) chain A residue 41 type sequence R description binding site for Di-peptide ZS8 C 425 and LEU C 426 source : AC3 7) chain A residue 42 type sequence N description binding site for Di-peptide ZS8 C 425 and LEU C 426 source : AC3 8) chain A residue 45 type sequence S description binding site for Di-peptide ZS8 C 425 and LEU C 426 source : AC3 9) chain A residue 120 type sequence K description binding site for Di-peptide ZS8 C 425 and LEU C 426 source : AC3 10) chain A residue 165 type sequence P description binding site for Di-peptide ZS8 C 425 and LEU C 426 source : AC3 11) chain A residue 3 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 12) chain A residue 68 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 13) chain A residue 56 type SITE sequence R description Interaction with phosphoserine on interacting protein => ECO:0000250|UniProtKB:P63103 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 127 type SITE sequence R description Interaction with phosphoserine on interacting protein => ECO:0000250|UniProtKB:P63103 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 210 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P63102 source Swiss-Prot : SWS_FT_FI7 16) chain A residue 1 type MOD_RES sequence M description N-acetylmethionine => ECO:0000269|Ref.8, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 58 type MOD_RES sequence S description Phosphoserine; by PKA and PKB/AKT1 => ECO:0000269|PubMed:11956222, ECO:0000269|PubMed:12865427, ECO:0000269|PubMed:15883165, ECO:0000269|PubMed:16376338 source Swiss-Prot : SWS_FT_FI4 18) chain A residue 184 type MOD_RES sequence S description Phosphoserine; by MAPK8 => ECO:0000269|PubMed:15071501, ECO:0000269|PubMed:15696159 source Swiss-Prot : SWS_FT_FI5 19) chain A residue 41-51 type prosite sequence RNLLSVAYKNV description 1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV source prosite : PS00796 20) chain A residue 211-230 type prosite sequence YKDSTLIMQLLRDNLTLWTS description 1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS source prosite : PS00797

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