eF-site ID 6i3y-ACFH PDB Code 6i3y Chain A, C, F, H click to enlarge Title Crystal structure of the human mitochondrial PRELID1K58V-TRIAP1 complex with PS Classification LIPID TRANSPORT Compound PRELI domain-containing protein 1, mitochondrial Source (TRIA1_HUMAN) Sequence A:  DDKMNSVGEACTDMKREYDQCFNRWFAEKFLKGDSSGDPC TDLFKRYQQCVQKAIKEKEIPIEGLEFMGHGKEK C:  QMVKYFLGQSVLRSSWDQVFAAFWQRYPNPYSKHVLTEDI VHREVTPDQKLLSRRLLTVTNRMPRWAERLFPANVAHSVY VLEDSIVDPQNQTMTTFTWNINHARLMVVEERSVYSVNSD NSGWTEIRREAWVSSSLFGVSRAVQEFGLARFKSNVTKTM KGFEYILAKLQGE F:  SHHHHHHSDQMVKYFLGQSVLRSSWDQVFAAFWQRYPNPY SKHVLTEDIVHREVTPDQKLLSRRLLTVTNRMPRWAERLF PANVAHSVYVLEDSIVDPQNQTMTTFTWNINHARLMVVEE RSVYSVNSDNSGWTEIRREAWVSSSLFGVSRAVQEFGLAR FKSNVTKTMKGFEYILAKLQGE H:  DKMNSVGEACTDMKREYDQCFNRWFAEKFLKGDSSGDPCT DLFKRYQQCVQKAIKEKEIPIEGLEFMG Description Functional site 1) chain C residue 120 type sequence E description binding site for residue LMT C 201 source : AC1 2) chain C residue 71 type sequence N description binding site for residue P5S C 202 source : AC2 3) chain C residue 73 type sequence M description binding site for residue P5S C 202 source : AC2 4) chain C residue 89 type sequence V description binding site for residue P5S C 202 source : AC2 5) chain C residue 91 type sequence V description binding site for residue P5S C 202 source : AC2 6) chain C residue 108 type sequence T description binding site for residue P5S C 202 source : AC2 7) chain C residue 110 type sequence N description binding site for residue P5S C 202 source : AC2 8) chain C residue 113 type sequence H description binding site for residue P5S C 202 source : AC2 9) chain C residue 117 type sequence M description binding site for residue P5S C 202 source : AC2 10) chain C residue 119 type sequence V description binding site for residue P5S C 202 source : AC2 11) chain C residue 121 type sequence E description binding site for residue P5S C 202 source : AC2 12) chain F residue 161 type sequence R description binding site for residue P5S C 202 source : AC2 13) chain C residue 161 type sequence R description binding site for residue P5S F 201 source : AC3 14) chain C residue 165 type sequence N description binding site for residue P5S F 201 source : AC3 15) chain C residue 169 type sequence T description binding site for residue P5S F 201 source : AC3 16) chain F residue 36 type sequence R description binding site for residue P5S F 201 source : AC3 17) chain F residue 37 type sequence Y description binding site for residue P5S F 201 source : AC3 18) chain F residue 39 type sequence N description binding site for residue P5S F 201 source : AC3 19) chain F residue 41 type sequence Y description binding site for residue P5S F 201 source : AC3 20) chain F residue 42 type sequence S description binding site for residue P5S F 201 source : AC3 21) chain F residue 44 type sequence H description binding site for residue P5S F 201 source : AC3 22) chain F residue 69 type sequence V description binding site for residue P5S F 201 source : AC3 23) chain F residue 70 type sequence T description binding site for residue P5S F 201 source : AC3 24) chain F residue 71 type sequence N description binding site for residue P5S F 201 source : AC3 25) chain F residue 72 type sequence R description binding site for residue P5S F 201 source : AC3 26) chain F residue 73 type sequence M description binding site for residue P5S F 201 source : AC3 27) chain F residue 89 type sequence V description binding site for residue P5S F 201 source : AC3 28) chain F residue 91 type sequence V description binding site for residue P5S F 201 source : AC3 29) chain F residue 110 type sequence N description binding site for residue P5S F 201 source : AC3 30) chain F residue 113 type sequence H description binding site for residue P5S F 201 source : AC3 31) chain F residue 117 type sequence M description binding site for residue P5S F 201 source : AC3 32) chain F residue 119 type sequence V description binding site for residue P5S F 201 source : AC3 33) chain A residue 40 type SITE sequence F description Important for interaction with PRELID3A => ECO:0000269|PubMed:26071602 source Swiss-Prot : SWS_FT_FI1 34) chain A residue 54 type SITE sequence F description Important for interaction with PRELID3A => ECO:0000269|PubMed:26071602 source Swiss-Prot : SWS_FT_FI1 35) chain H residue 40 type SITE sequence F description Important for interaction with PRELID3A => ECO:0000269|PubMed:26071602 source Swiss-Prot : SWS_FT_FI1 36) chain H residue 54 type SITE sequence F description Important for interaction with PRELID3A => ECO:0000269|PubMed:26071602 source Swiss-Prot : SWS_FT_FI1 37) 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 38) chain H residue 14 type MOD_RES sequence M description N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI2

Display surface Download Links