eF-site ID 6r8w-A
PDB Code 6r8w
Chain A

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Title Human Cyclophilin D in complex with 2-(exo-3,5-Dioxo-4-aza-tricyclo[5.2.1.02,6]dec-4-yl)-N-((1R,9R,10S)-10-hydroxy-12-oxa-8-aza-tricyclo[7.3.1.02,7]trideca-2(7),3,5-trien-4-ylmethyl)-acetamide
Classification ISOMERASE
Compound Peptidyl-prolyl cis-trans isomerase F, mitochondrial
Source (PPIF_HUMAN)
Sequence A:  GNPLVYLDVDANGKPLGRVVLELKADVVPKTAENFRALCT
GEKGFGYKGSTFHRVIPSFMCQAGDFTNHNGTGGKSIYGS
RFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDW
LDGKHVVFGHVIEGMDVVKKIESFGSKSGRTSKKIVITDC
GQLS
Description


Functional site

1) chain A
residue 101
type
sequence S
description binding site for residue O4B A 301
source : AC1

2) chain A
residue 101
type
sequence S
description binding site for residue O4B A 301
source : AC1

3) chain A
residue 102
type
sequence F
description binding site for residue O4B A 301
source : AC1

4) chain A
residue 102
type
sequence F
description binding site for residue O4B A 301
source : AC1

5) chain A
residue 190
type
sequence K
description binding site for residue O4B A 301
source : AC1

6) chain A
residue 190
type
sequence K
description binding site for residue O4B A 301
source : AC1

7) chain A
residue 88
type
sequence F
description binding site for residue P6G A 302
source : AC2

8) chain A
residue 120
type
sequence I
description binding site for residue P6G A 302
source : AC2

9) chain A
residue 121
type
sequence Y
description binding site for residue P6G A 302
source : AC2

10) chain A
residue 135
type
sequence V
description binding site for residue P6G A 302
source : AC2

11) chain A
residue 137
type
sequence P
description binding site for residue P6G A 302
source : AC2

12) chain A
residue 173
type
sequence H
description binding site for residue P6G A 302
source : AC2

13) chain A
residue 97
type
sequence R
description binding site for residue JVH A 303
source : AC3

14) chain A
residue 97
type
sequence R
description binding site for residue JVH A 303
source : AC3

15) chain A
residue 102
type
sequence F
description binding site for residue JVH A 303
source : AC3

16) chain A
residue 105
type
sequence Q
description binding site for residue JVH A 303
source : AC3

17) chain A
residue 114
type
sequence G
description binding site for residue JVH A 303
source : AC3

18) chain A
residue 115
type
sequence T
description binding site for residue JVH A 303
source : AC3

19) chain A
residue 115
type
sequence T
description binding site for residue JVH A 303
source : AC3

20) chain A
residue 116
type
sequence G
description binding site for residue JVH A 303
source : AC3

21) chain A
residue 123
type
sequence S
description binding site for residue JVH A 303
source : AC3

22) chain A
residue 124
type
sequence R
description binding site for residue JVH A 303
source : AC3

23) chain A
residue 143
type
sequence A
description binding site for residue JVH A 303
source : AC3

24) chain A
residue 144
type
sequence N
description binding site for residue JVH A 303
source : AC3

25) chain A
residue 149
type
sequence T
description binding site for residue JVH A 303
source : AC3

26) chain A
residue 151
type
sequence G
description binding site for residue JVH A 303
source : AC3

27) chain A
residue 153
type
sequence Q
description binding site for residue JVH A 303
source : AC3

28) chain A
residue 155
type
sequence F
description binding site for residue JVH A 303
source : AC3

29) chain A
residue 168
type
sequence H
description binding site for residue JVH A 303
source : AC3

30) chain A
residue 90-107
type prosite
sequence YKGSTFHRVIPSFMCQAG
description CSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YkgStFHRVIpsFMcQAG
source prosite : PS00170

31) chain A
residue 67
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KR7
source Swiss-Prot : SWS_FT_FI1

32) chain A
residue 86
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q99KR7
source Swiss-Prot : SWS_FT_FI2

33) chain A
residue 175
type MOD_RES
sequence I
description N6-succinyllysine => ECO:0000250|UniProtKB:Q99KR7
source Swiss-Prot : SWS_FT_FI2

34) chain A
residue 190
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q99KR7
source Swiss-Prot : SWS_FT_FI2

35) chain A
residue 167
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:Q99KR7
source Swiss-Prot : SWS_FT_FI3

36) chain A
residue 203
type MOD_RES
sequence C
description S-nitrosocysteine => ECO:0000250|UniProtKB:Q99KR7
source Swiss-Prot : SWS_FT_FI4


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