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


Display surface

Download
Links