eF-site ID 6i3y-ACFH
PDB Code 6i3y
Chain A, C, F, H

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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


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