eF-site ID 3w9p-AB PDB Code 3w9p Chain A, B click to enlarge Title Crystal structure of monomeric FraC (second crystal form) Classification TOXIN Compound Fragaceatoxin C Source Actinia fragacea (Strawberry anemone) (ACTPC_ACTFR) Sequence A:  AGAVIDGAGLGFDVLKTVLEALGNVKRKIAVGIDNESGKT WTAMNTYFRSGTSDIVLPHKVAHGKALLYNGQKNRGPVAT GVVGVIAYSMSDGNTLAVLFSVPYDYNWYSNWWNVRVYKG QKRADQRMYEELYYHRSPFRGDNGWHSRGLGYGLKSRGFM NSSGHAILEIHVTKA B:  GAVIDGAGLGFDVLKTVLEALGNVKRKIAVGIDNESGKTW TAMNTYFRSGTSDIVLPHKVAHGKALLYNGQKNRGPVATG VVGVIAYSMSDGNTLAVLFSVPYDYNWYSNWWNVRVYKGQ KRADQRMYEELYYHRSPFRGDNGWHSRGLGYGLKSRGFMN SSGHAILEIHVTKA Description Functional site 1) chain A 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 A 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 31 type BINDING sequence R description in subunit A; in oligomeric forms only => ECO:0000305|PubMed:25716479 source Swiss-Prot : SWS_FT_FI1 4) 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 5) chain A residue 51 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:28630155 source Swiss-Prot : SWS_FT_FI2 6) chain A residue 53 type BINDING sequence R description BINDING => ECO:0000269|PubMed:28630155 source Swiss-Prot : SWS_FT_FI2 7) chain A residue 138 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:28630155 source Swiss-Prot : SWS_FT_FI2 8) chain B residue 51 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:28630155 source Swiss-Prot : SWS_FT_FI2 9) chain B residue 53 type BINDING sequence R description BINDING => ECO:0000269|PubMed:28630155 source Swiss-Prot : SWS_FT_FI2 10) chain B residue 138 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:28630155 source Swiss-Prot : SWS_FT_FI2 11) chain A residue 54 type BINDING sequence S description in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479 source Swiss-Prot : SWS_FT_FI3 12) chain B residue 54 type BINDING sequence S description in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479 source Swiss-Prot : SWS_FT_FI3 13) chain B residue 85 type BINDING sequence G description in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479 source Swiss-Prot : SWS_FT_FI3 14) chain B residue 108 type BINDING sequence Y description in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479 source Swiss-Prot : SWS_FT_FI3 15) chain B residue 113 type BINDING sequence Y description in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479 source Swiss-Prot : SWS_FT_FI3 16) chain B residue 114 type BINDING sequence S description in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479 source Swiss-Prot : SWS_FT_FI3 17) chain B residue 116 type BINDING sequence W description in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479 source Swiss-Prot : SWS_FT_FI3 18) chain B residue 133 type BINDING sequence Y description in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479 source Swiss-Prot : SWS_FT_FI3 19) chain B residue 137 type BINDING sequence Y description in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479 source Swiss-Prot : SWS_FT_FI3 20) chain B residue 144 type BINDING sequence R description in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 85 type BINDING sequence G description in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 108 type BINDING sequence Y description in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 113 type BINDING sequence Y description in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 114 type BINDING sequence S description in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 116 type BINDING sequence W description in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 133 type BINDING sequence Y description in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479 source Swiss-Prot : SWS_FT_FI3 27) chain A residue 137 type BINDING sequence Y description in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479 source Swiss-Prot : SWS_FT_FI3 28) chain A residue 144 type BINDING sequence R description in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479 source Swiss-Prot : SWS_FT_FI3 29) chain A residue 79 type BINDING sequence R description in subunit B; in oligomeric forms only => ECO:0000305|PubMed:25716479 source Swiss-Prot : SWS_FT_FI4 30) 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 31) chain A 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 32) 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 33) chain A 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 34) 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 35) chain A 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 36) 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 37) chain A 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 38) 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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