eF-site ID 3w9p-B
PDB Code 3w9p
Chain B

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Title Crystal structure of monomeric FraC (second crystal form)
Classification TOXIN
Compound Fragaceatoxin C
Source Actinia fragacea (Strawberry anemone) (ACTPC_ACTFR)
Sequence B:  GAVIDGAGLGFDVLKTVLEALGNVKRKIAVGIDNESGKTW
TAMNTYFRSGTSDIVLPHKVAHGKALLYNGQKNRGPVATG
VVGVIAYSMSDGNTLAVLFSVPYDYNWYSNWWNVRVYKGQ
KRADQRMYEELYYHRSPFRGDNGWHSRGLGYGLKSRGFMN
SSGHAILEIHVTKA
Description


Functional site

1) chain B
residue 31
type BINDING
sequence R
description in subunit A; in oligomeric forms only => ECO:0000305|PubMed:25716479
source Swiss-Prot : SWS_FT_FI1

2) chain B
residue 168
type BINDING
sequence G
description in subunit A; in oligomeric forms only => ECO:0000305|PubMed:25716479
source Swiss-Prot : SWS_FT_FI1

3) chain B
residue 51
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:28630155
source Swiss-Prot : SWS_FT_FI2

4) chain B
residue 53
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:28630155
source Swiss-Prot : SWS_FT_FI2

5) chain B
residue 138
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:28630155
source Swiss-Prot : SWS_FT_FI2

6) chain B
residue 54
type BINDING
sequence S
description in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479
source Swiss-Prot : SWS_FT_FI3

7) chain B
residue 85
type BINDING
sequence G
description in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479
source Swiss-Prot : SWS_FT_FI3

8) chain B
residue 108
type BINDING
sequence Y
description in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479
source Swiss-Prot : SWS_FT_FI3

9) chain B
residue 113
type BINDING
sequence Y
description in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479
source Swiss-Prot : SWS_FT_FI3

10) chain B
residue 114
type BINDING
sequence S
description in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479
source Swiss-Prot : SWS_FT_FI3

11) chain B
residue 116
type BINDING
sequence W
description in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479
source Swiss-Prot : SWS_FT_FI3

12) chain B
residue 133
type BINDING
sequence Y
description in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479
source Swiss-Prot : SWS_FT_FI3

13) chain B
residue 137
type BINDING
sequence Y
description in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479
source Swiss-Prot : SWS_FT_FI3

14) chain B
residue 144
type BINDING
sequence R
description in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479
source Swiss-Prot : SWS_FT_FI3

15) chain B
residue 79
type BINDING
sequence R
description in subunit B; in oligomeric forms only => ECO:0000305|PubMed:25716479
source Swiss-Prot : SWS_FT_FI4

16) chain B
residue 16
type SITE
sequence F
description Part of the hydrophobic cavity (in subunit A) that receives Val-60 from the adjacent subunit (B); essential in hemolysis, since it is critical for pore formation in cholesterol-rich membrane cells (such as red blood cells) => ECO:0000305|PubMed:21300287, ECO:0000305|PubMed:25716479, ECO:0000305|PubMed:25759390
source Swiss-Prot : SWS_FT_FI5

17) chain B
residue 60
type SITE
sequence V
description Protrudes from one subunit (B) and inserts into the hydrophobic cavity from the adjacent subunit (A) => ECO:0000305|PubMed:21300287, ECO:0000305|PubMed:25716479
source Swiss-Prot : SWS_FT_FI6

18) chain B
residue 149
type SITE
sequence W
description Part of the hydrophobic cavity (in subunit A) that receives Val-60 from the adjacent subunit (B) => ECO:0000305|PubMed:21300287, ECO:0000305|PubMed:25716479
source Swiss-Prot : SWS_FT_FI7

19) chain B
residue 163
type SITE
sequence F
description Part of the hydrophobic cavity (in subunit A) that receives Val-60 from the adjacent subunit (B) => ECO:0000305|PubMed:21300287
source Swiss-Prot : SWS_FT_FI8


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