eF-site ID 6a5s-ABCDEFGH PDB Code 6a5s Chain A, B, C, D, E, F, G, H click to enlarge Title Structure of 14-3-3 gamma in complex with TFEB 14-3-3 binding motif Classification TRANSCRIPTION Compound 14-3-3 protein gamma Source (6A5S) Sequence A:  VDREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEE RNLLSVAYKNVVGARRSSWRVISSIEQKTNEKKIEMVRAY REKIEKELEAVCQDVLSLLDNYLIKNCSETQYESKVFYLK MKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHM QPTHPIRLGLALNYSVFYYEIQNAPEQACHLAKTAFDDAI AELDTLNEDSYKDSTLIMQLLRDNLTLWTS B:  DREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEER NLLSVAYKNVVGARRSSWRVISSIEQKTNEKKIEMVRAYR EKIEKELEAVCQDVLSLLDNYLIKNCSETQYESKVFYLKM KGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQ PTHPIRLGLALNYSVFYYEIQNAPEQACHLAKTAFDDAIA ELDTLNEDSYKDSTLIMQLLRDNLTLWTS C:  VTSSXCPADLT D:  DREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEER NLLSVAYKNVVGARRSSWRVISSIEQKTSADGNEKKIEMV RAYREKIEKELEAVCQDVLSLLDNYLIKNCSETQYESKVF YLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISK EHMQPTHPIRLGLALNYSVFYYEIQNAPEQACHLAKTAFD DAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTS E:  VTSSXCPADLT F:  VTSSXCPADLT G:  DREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEER NLLSVAYKNVVGARRSSWRVISSIEQKTEKKIEMVRAYRE KIEKELEAVCQDVLSLLDNYLIKNCSETQYESKVFYLKMK GDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQP THPIRLGLALNYSVFYYEIQNAPEQACHLAKTAFDDAIAE LDTLNEDSYKDSTLIMQLLRDNLTLWTS H:  VTSSXCPADLT Description Functional site 1) chain A residue 120 type sequence K description binding site for residue NA A 301 source : AC1 2) chain B residue 202 type sequence D description binding site for residue MG B 301 source : AC2 3) chain B residue 203 type sequence D description binding site for residue MG B 301 source : AC2 4) chain B residue 204 type sequence A description binding site for residue MG B 301 source : AC2 5) chain B residue 205 type sequence I description binding site for residue MG B 301 source : AC2 6) chain B residue 206 type sequence A description binding site for residue MG B 301 source : AC2 7) chain B residue 50 type sequence K description binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5 source : AC3 8) chain B residue 57 type sequence R description binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5 source : AC3 9) chain B residue 132 type sequence R description binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5 source : AC3 10) chain B residue 133 type sequence Y description binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5 source : AC3 11) chain B residue 174 type sequence G description binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5 source : AC3 12) chain B residue 177 type sequence L description binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5 source : AC3 13) chain B residue 178 type sequence N description binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5 source : AC3 14) chain B residue 225 type sequence L description binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5 source : AC3 15) chain C residue 5 type sequence S description binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5 source : AC3 16) chain C residue 8 type sequence P description binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5 source : AC3 17) chain A residue 50 type sequence K description binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5 source : AC4 18) chain A residue 57 type sequence R description binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5 source : AC4 19) chain A residue 132 type sequence R description binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5 source : AC4 20) chain A residue 133 type sequence Y description binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5 source : AC4 21) chain A residue 174 type sequence G description binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5 source : AC4 22) chain A residue 177 type sequence L description binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5 source : AC4 23) chain A residue 178 type sequence N description binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5 source : AC4 24) chain A residue 225 type sequence L description binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5 source : AC4 25) chain E residue 5 type sequence S description binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5 source : AC4 26) chain E residue 8 type sequence P description binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5 source : AC4 27) chain E residue 9 type sequence A description binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5 source : AC4 28) chain D residue 50 type sequence K description binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5 source : AC5 29) chain D residue 57 type sequence R description binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5 source : AC5 30) chain D residue 132 type sequence R description binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5 source : AC5 31) chain D residue 133 type sequence Y description binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5 source : AC5 32) chain D residue 174 type sequence G description binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5 source : AC5 33) chain D residue 177 type sequence L description binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5 source : AC5 34) chain D residue 178 type sequence N description binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5 source : AC5 35) chain F residue 5 type sequence S description binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5 source : AC5 36) chain F residue 8 type sequence P description binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5 source : AC5 37) chain F residue 9 type sequence A description binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5 source : AC5 38) chain G residue 50 type sequence K description binding site for Ligand residues SEP H 6 through CYS H 7 bound to SER H 5 source : AC6 39) chain G residue 57 type sequence R description binding site for Ligand residues SEP H 6 through CYS H 7 bound to SER H 5 source : AC6 40) chain G residue 132 type sequence R description binding site for Ligand residues SEP H 6 through CYS H 7 bound to SER H 5 source : AC6 41) chain G residue 133 type sequence Y description binding site for Ligand residues SEP H 6 through CYS H 7 bound to SER H 5 source : AC6 42) chain G residue 174 type sequence G description binding site for Ligand residues SEP H 6 through CYS H 7 bound to SER H 5 source : AC6 43) chain G residue 177 type sequence L description binding site for Ligand residues SEP H 6 through CYS H 7 bound to SER H 5 source : AC6 44) chain G residue 178 type sequence N description binding site for Ligand residues SEP H 6 through CYS H 7 bound to SER H 5 source : AC6 45) chain H residue 5 type sequence S description binding site for Ligand residues SEP H 6 through CYS H 7 bound to SER H 5 source : AC6 46) chain H residue 8 type sequence P description binding site for Ligand residues SEP H 6 through CYS H 7 bound to SER H 5 source : AC6 47) chain A residue 42-52 type prosite sequence RNLLSVAYKNV description 1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV source prosite : PS00796 48) chain A residue 216-235 type prosite sequence YKDSTLIMQLLRDNLTLWTS description 1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS source prosite : PS00797 49) chain A residue 57 type SITE sequence R description Interaction with phosphoserine on interacting protein => ECO:0000269|PubMed:17085597 source Swiss-Prot : SWS_FT_FI1 50) chain A residue 132 type SITE sequence R description Interaction with phosphoserine on interacting protein => ECO:0000269|PubMed:17085597 source Swiss-Prot : SWS_FT_FI1 51) chain B residue 57 type SITE sequence R description Interaction with phosphoserine on interacting protein => ECO:0000269|PubMed:17085597 source Swiss-Prot : SWS_FT_FI1 52) chain B residue 132 type SITE sequence R description Interaction with phosphoserine on interacting protein => ECO:0000269|PubMed:17085597 source Swiss-Prot : SWS_FT_FI1 53) chain D residue 57 type SITE sequence R description Interaction with phosphoserine on interacting protein => ECO:0000269|PubMed:17085597 source Swiss-Prot : SWS_FT_FI1 54) chain D residue 132 type SITE sequence R description Interaction with phosphoserine on interacting protein => ECO:0000269|PubMed:17085597 source Swiss-Prot : SWS_FT_FI1 55) chain G residue 57 type SITE sequence R description Interaction with phosphoserine on interacting protein => ECO:0000269|PubMed:17085597 source Swiss-Prot : SWS_FT_FI1 56) chain G residue 132 type SITE sequence R description Interaction with phosphoserine on interacting protein => ECO:0000269|PubMed:17085597 source Swiss-Prot : SWS_FT_FI1 57) chain A residue 2 type MOD_RES sequence V description N-acetylvaline; partial => ECO:0000269|PubMed:14534293, ECO:0000269|Ref.7, ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330 source Swiss-Prot : SWS_FT_FI3 58) chain D residue 71 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI4 59) chain A residue 133 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P61983 source Swiss-Prot : SWS_FT_FI5 60) chain B residue 133 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P61983 source Swiss-Prot : SWS_FT_FI5 61) chain D residue 133 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P61983 source Swiss-Prot : SWS_FT_FI5 62) chain G residue 133 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P61983 source Swiss-Prot : SWS_FT_FI5 63) chain A residue 145 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|Ref.7 source Swiss-Prot : SWS_FT_FI6 64) chain B residue 145 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|Ref.7 source Swiss-Prot : SWS_FT_FI6 65) chain D residue 145 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|Ref.7 source Swiss-Prot : SWS_FT_FI6 66) chain G residue 145 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|Ref.7 source Swiss-Prot : SWS_FT_FI6 67) chain A residue 215 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P61983 source Swiss-Prot : SWS_FT_FI7 68) chain B residue 215 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P61983 source Swiss-Prot : SWS_FT_FI7 69) chain D residue 215 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P61983 source Swiss-Prot : SWS_FT_FI7 70) chain G residue 215 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P61983 source Swiss-Prot : SWS_FT_FI7 71) chain A residue 234 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 72) chain B residue 234 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 73) chain D residue 234 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 74) chain G residue 234 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 75) chain A residue 235 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 76) chain B residue 235 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 77) chain D residue 235 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 78) chain G residue 235 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9

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