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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9GKL

Structure of the octameric pore of Fragaceotxin C (FraC or DELTA-actitoxin-Afr1a) in large unilamellar vesicles.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0006811biological_processmonoatomic ion transport
A0008289molecular_functionlipid binding
A0031640biological_processkilling of cells of another organism
A0035821biological_processmodulation of process of another organism
A0042151cellular_componentnematocyst
A0042802molecular_functionidentical protein binding
A0044218cellular_componentother organism cell membrane
A0055085biological_processtransmembrane transport
A0090729molecular_functiontoxin activity
B0005576cellular_componentextracellular region
B0006811biological_processmonoatomic ion transport
B0008289molecular_functionlipid binding
B0031640biological_processkilling of cells of another organism
B0035821biological_processmodulation of process of another organism
B0042151cellular_componentnematocyst
B0042802molecular_functionidentical protein binding
B0044218cellular_componentother organism cell membrane
B0055085biological_processtransmembrane transport
B0090729molecular_functiontoxin activity
C0005576cellular_componentextracellular region
C0006811biological_processmonoatomic ion transport
C0008289molecular_functionlipid binding
C0031640biological_processkilling of cells of another organism
C0035821biological_processmodulation of process of another organism
C0042151cellular_componentnematocyst
C0042802molecular_functionidentical protein binding
C0044218cellular_componentother organism cell membrane
C0055085biological_processtransmembrane transport
C0090729molecular_functiontoxin activity
D0005576cellular_componentextracellular region
D0006811biological_processmonoatomic ion transport
D0008289molecular_functionlipid binding
D0031640biological_processkilling of cells of another organism
D0035821biological_processmodulation of process of another organism
D0042151cellular_componentnematocyst
D0042802molecular_functionidentical protein binding
D0044218cellular_componentother organism cell membrane
D0055085biological_processtransmembrane transport
D0090729molecular_functiontoxin activity
E0005576cellular_componentextracellular region
E0006811biological_processmonoatomic ion transport
E0008289molecular_functionlipid binding
E0031640biological_processkilling of cells of another organism
E0035821biological_processmodulation of process of another organism
E0042151cellular_componentnematocyst
E0042802molecular_functionidentical protein binding
E0044218cellular_componentother organism cell membrane
E0055085biological_processtransmembrane transport
E0090729molecular_functiontoxin activity
F0005576cellular_componentextracellular region
F0006811biological_processmonoatomic ion transport
F0008289molecular_functionlipid binding
F0031640biological_processkilling of cells of another organism
F0035821biological_processmodulation of process of another organism
F0042151cellular_componentnematocyst
F0042802molecular_functionidentical protein binding
F0044218cellular_componentother organism cell membrane
F0055085biological_processtransmembrane transport
F0090729molecular_functiontoxin activity
G0005576cellular_componentextracellular region
G0006811biological_processmonoatomic ion transport
G0008289molecular_functionlipid binding
G0031640biological_processkilling of cells of another organism
G0035821biological_processmodulation of process of another organism
G0042151cellular_componentnematocyst
G0042802molecular_functionidentical protein binding
G0044218cellular_componentother organism cell membrane
G0055085biological_processtransmembrane transport
G0090729molecular_functiontoxin activity
U0005576cellular_componentextracellular region
U0006811biological_processmonoatomic ion transport
U0008289molecular_functionlipid binding
U0031640biological_processkilling of cells of another organism
U0035821biological_processmodulation of process of another organism
U0042151cellular_componentnematocyst
U0042802molecular_functionidentical protein binding
U0044218cellular_componentother organism cell membrane
U0055085biological_processtransmembrane transport
U0090729molecular_functiontoxin activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues120
DetailsRegion: {"description":"Trp-rich region, which is important for the binding to lipid membrane","evidences":[{"source":"UniProtKB","id":"P61914","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues16
DetailsMotif: {"description":"Cell attachment site, crucial for protein stability","evidences":[{"source":"UniProtKB","id":"P07845","evidenceCode":"ECO:0000250"},{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"description":"in subunit A; in oligomeric forms only","evidences":[{"source":"PubMed","id":"25716479","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28630155","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues72
DetailsBinding site: {"description":"in monomeric and oligomeric forms","evidences":[{"source":"PubMed","id":"25716479","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues8
DetailsBinding site: {"description":"in subunit B; in oligomeric forms only","evidences":[{"source":"PubMed","id":"25716479","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues8
DetailsSite: {"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)","evidences":[{"source":"PubMed","id":"21300287","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25716479","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25759390","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues8
DetailsSite: {"description":"Protrudes from one subunit (B) and inserts into the hydrophobic cavity from the adjacent subunit (A)","evidences":[{"source":"PubMed","id":"21300287","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25716479","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues8
DetailsSite: {"description":"Part of the hydrophobic cavity (in subunit A) that receives Val-60 from the adjacent subunit (B)","evidences":[{"source":"PubMed","id":"21300287","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25716479","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues8
DetailsSite: {"description":"Part of the hydrophobic cavity (in subunit A) that receives Val-60 from the adjacent subunit (B)","evidences":[{"source":"PubMed","id":"21300287","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

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PDB entries from 2026-01-14

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