eF-site ID 5j31-ABCD PDB Code 5j31 Chain A, B, C, D 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 B:  MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEE RNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAR EYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLK MKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEM QPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAI AELDTLEESYKDSTLIMQLLRDNLTLWTS C:  GXLDXLDLAS D:  GXLDXLDLAS Description Functional site 1) chain A residue 222 type sequence R description binding site for residue BEZ B 301 source : AC1 2) chain B residue 219 type sequence Q description binding site for residue BEZ B 301 source : AC1 3) chain B residue 222 type sequence R description binding site for residue BEZ B 301 source : AC1 4) chain A residue 41 type sequence R description binding site for Di-peptide ASP C 424 and ZS8 C 425 source : AC2 5) chain A residue 42 type sequence N description binding site for Di-peptide ASP C 424 and ZS8 C 425 source : AC2 6) chain A residue 45 type sequence S description binding site for Di-peptide ASP C 424 and ZS8 C 425 source : AC2 7) chain A residue 49 type sequence K description binding site for Di-peptide ASP C 424 and ZS8 C 425 source : AC2 8) chain C residue 421 type sequence G description binding site for Di-peptide ASP C 424 and ZS8 C 425 source : AC2 9) chain C residue 422 type sequence X description binding site for Di-peptide ASP C 424 and ZS8 C 425 source : AC2 10) chain C residue 423 type sequence L description binding site for Di-peptide ASP C 424 and ZS8 C 425 source : AC2 11) chain C residue 426 type sequence L description binding site for Di-peptide ASP C 424 and ZS8 C 425 source : AC2 12) chain C residue 427 type sequence D description binding site for Di-peptide ASP C 424 and ZS8 C 425 source : AC2 13) chain A residue 41 type sequence R description binding site for Di-peptide ZS8 C 425 and LEU C 426 source : AC3 14) chain A residue 42 type sequence N description binding site for Di-peptide ZS8 C 425 and LEU C 426 source : AC3 15) chain A residue 45 type sequence S description binding site for Di-peptide ZS8 C 425 and LEU C 426 source : AC3 16) chain A residue 120 type sequence K description binding site for Di-peptide ZS8 C 425 and LEU C 426 source : AC3 17) chain A residue 165 type sequence P description binding site for Di-peptide ZS8 C 425 and LEU C 426 source : AC3 18) chain C residue 422 type sequence X description binding site for Di-peptide ZS8 C 425 and LEU C 426 source : AC3 19) chain C residue 423 type sequence L description binding site for Di-peptide ZS8 C 425 and LEU C 426 source : AC3 20) chain C residue 424 type sequence D description binding site for Di-peptide ZS8 C 425 and LEU C 426 source : AC3 21) chain C residue 427 type sequence D description binding site for Di-peptide ZS8 C 425 and LEU C 426 source : AC3 22) chain C residue 428 type sequence L description binding site for Di-peptide ZS8 C 425 and LEU C 426 source : AC3 23) chain B residue 41 type sequence R description binding site for Di-peptide ASP D 424 and ZS8 D 425 source : AC4 24) chain B residue 42 type sequence N description binding site for Di-peptide ASP D 424 and ZS8 D 425 source : AC4 25) chain B residue 49 type sequence K description binding site for Di-peptide ASP D 424 and ZS8 D 425 source : AC4 26) chain B residue 117 type sequence F description binding site for Di-peptide ASP D 424 and ZS8 D 425 source : AC4 27) chain D residue 421 type sequence G description binding site for Di-peptide ASP D 424 and ZS8 D 425 source : AC4 28) chain D residue 422 type sequence X description binding site for Di-peptide ASP D 424 and ZS8 D 425 source : AC4 29) chain D residue 423 type sequence L description binding site for Di-peptide ASP D 424 and ZS8 D 425 source : AC4 30) chain D residue 426 type sequence L description binding site for Di-peptide ASP D 424 and ZS8 D 425 source : AC4 31) chain D residue 427 type sequence D description binding site for Di-peptide ASP D 424 and ZS8 D 425 source : AC4 32) chain B residue 41 type sequence R description binding site for Di-peptide ZS8 D 425 and LEU D 426 source : AC5 33) chain B residue 42 type sequence N description binding site for Di-peptide ZS8 D 425 and LEU D 426 source : AC5 34) chain B residue 117 type sequence F description binding site for Di-peptide ZS8 D 425 and LEU D 426 source : AC5 35) chain B residue 120 type sequence K description binding site for Di-peptide ZS8 D 425 and LEU D 426 source : AC5 36) chain D residue 422 type sequence X description binding site for Di-peptide ZS8 D 425 and LEU D 426 source : AC5 37) chain D residue 423 type sequence L description binding site for Di-peptide ZS8 D 425 and LEU D 426 source : AC5 38) chain D residue 424 type sequence D description binding site for Di-peptide ZS8 D 425 and LEU D 426 source : AC5 39) chain D residue 427 type sequence D description binding site for Di-peptide ZS8 D 425 and LEU D 426 source : AC5 40) chain D residue 428 type sequence L description binding site for Di-peptide ZS8 D 425 and LEU D 426 source : AC5 41) 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 42) 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 43) chain B residue 56 type SITE sequence R description Interaction with phosphoserine on interacting protein => ECO:0000250|UniProtKB:P63103 source Swiss-Prot : SWS_FT_FI1 44) chain B residue 127 type SITE sequence R description Interaction with phosphoserine on interacting protein => ECO:0000250|UniProtKB:P63103 source Swiss-Prot : SWS_FT_FI1 45) 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 46) chain B 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 47) chain A residue 3 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 48) chain A residue 68 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 49) chain B residue 3 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 50) chain B residue 68 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 51) 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 52) chain B 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 53) 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 54) chain B 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 55) chain A residue 210 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P63102 source Swiss-Prot : SWS_FT_FI7 56) chain B residue 210 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P63102 source Swiss-Prot : SWS_FT_FI7 57) chain A residue 41-51 type prosite sequence RNLLSVAYKNV description 1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV source prosite : PS00796 58) 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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