eF-site ID 6i3v-ABCF PDB Code 6i3v Chain A, B, C, F click to enlarge Title x-ray structure of the human mitochondrial PRELID1 in complex with TRIAP1 Classification LIPID BINDING PROTEIN Compound PRELI domain-containing protein 1, mitochondrial Source (TRIA1_HUMAN) Sequence A:  DKMNSVGEACTDMKREYDQCFNRWFAEKFLKGDSSGDPCT DLFKRYQQCVQKAIKEKEIPIEGLEFMGH B:  QMVKYFLGQSVLRSSWDQVFAAFWQRYPNPYSKHVLTEDI VHREVTPDQKLLSRRLLTKTNRMPRWAERLFPANVAHSVY VLEDSIVDPQNQTMTTFTWNINHARLMVVEERSVYSVNSD NSGWTEIRREAWVSSSLFGVSRAVQEFGLARFKSNVTKTM KGFEYILAKLQGE C:  DKMNSVGEACTDMKREYDQCFNRWFAEKFLKGDSSGDPCT DLFKRYQQCVQKAIKEKEIPIEGLEFMGH F:  HHHHHHSDQMVKYFLGQSVLRSSWDQVFAAFWQRYPNPYS KHVLTEDIVHREVTPDQKLLSRRLLTKTNRMPRWAERLFP ANVAHSVYVLEDSIVDPQNQTMTTFTWNINHARLMVVEER SVYSVNSDNSGWTEIRREAWVSSSLFGVSRAVQEFGLARF KSNVTKTMKGFEYILAKLQGEA Description (1)  PRELI domain-containing protein 1, mitochondrial, TP53-regulated inhibitor of apoptosis 1 Functional site 1) chain B residue 162 type sequence R description binding site for residue MYR F 201 source : AC1 2) chain B residue 163 type sequence F description binding site for residue MYR F 201 source : AC1 3) chain B residue 166 type sequence N description binding site for residue MYR F 201 source : AC1 4) chain F residue 72 type sequence N description binding site for residue MYR F 201 source : AC1 5) chain F residue 109 type sequence T description binding site for residue MYR F 201 source : AC1 6) chain F residue 111 type sequence N description binding site for residue MYR F 201 source : AC1 7) chain F residue 118 type sequence M description binding site for residue MYR F 201 source : AC1 8) chain F residue 120 type sequence V description binding site for residue MYR F 201 source : AC1 9) chain F residue 35 type sequence W description binding site for residue CL F 202 source : AC2 10) chain F residue 49 type sequence E description binding site for residue CL F 202 source : AC2 11) chain F residue 66 type sequence R description binding site for residue CL F 202 source : AC2 12) chain F residue 114 type sequence H description binding site for residue CL F 204 source : AC3 13) chain B residue 72 type sequence N description binding site for residue MYR B 201 source : AC4 14) chain B residue 90 type sequence V description binding site for residue MYR B 201 source : AC4 15) chain B residue 109 type sequence T description binding site for residue MYR B 201 source : AC4 16) chain B residue 111 type sequence N description binding site for residue MYR B 201 source : AC4 17) chain B residue 118 type sequence M description binding site for residue MYR B 201 source : AC4 18) chain B residue 120 type sequence V description binding site for residue MYR B 201 source : AC4 19) chain B residue 122 type sequence E description binding site for residue MYR B 201 source : AC4 20) chain F residue 162 type sequence R description binding site for residue MYR B 201 source : AC4 21) chain F residue 166 type sequence N description binding site for residue MYR B 201 source : AC4 22) chain F residue 170 type sequence T description binding site for residue MYR B 201 source : AC4 23) chain B residue 101 type sequence Q description binding site for residue NA B 202 source : AC5 24) chain B residue 114 type sequence H description binding site for residue CL B 207 source : AC9 25) chain B residue 73 type sequence R description binding site for residue CL B 211 source : AD2 26) chain F residue 166 type sequence N description binding site for residue CL B 211 source : AD2 27) chain F residue 83 type sequence P description binding site for residue CL B 213 source : AD3 28) chain F residue 84 type sequence A description binding site for residue CL B 213 source : AD3 29) chain A residue 40 type SITE sequence F description Important for interaction with PRELID3A => ECO:0000269|PubMed:26071602 source Swiss-Prot : SWS_FT_FI1 30) chain A residue 54 type SITE sequence F description Important for interaction with PRELID3A => ECO:0000269|PubMed:26071602 source Swiss-Prot : SWS_FT_FI1 31) chain C residue 40 type SITE sequence F description Important for interaction with PRELID3A => ECO:0000269|PubMed:26071602 source Swiss-Prot : SWS_FT_FI1 32) chain C residue 54 type SITE sequence F description Important for interaction with PRELID3A => ECO:0000269|PubMed:26071602 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 14 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI2 34) chain C residue 14 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI2

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