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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

3ZWJ

CRYSTAL STRUCTURE OF THE PORE-FORMING TOXIN FRAC FROM ACTINIA FRAGACEA (Form 3)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0006812biological_processmonoatomic cation transport
A0015267molecular_functionchannel activity
A0042151cellular_componentnematocyst
A0042802molecular_functionidentical protein binding
A0046930cellular_componentpore complex
A0046931biological_processpore complex assembly
A0051715biological_processcytolysis in another organism
A0055085biological_processtransmembrane transport
B0005576cellular_componentextracellular region
B0006812biological_processmonoatomic cation transport
B0015267molecular_functionchannel activity
B0042151cellular_componentnematocyst
B0042802molecular_functionidentical protein binding
B0046930cellular_componentpore complex
B0046931biological_processpore complex assembly
B0051715biological_processcytolysis in another organism
B0055085biological_processtransmembrane transport
C0005576cellular_componentextracellular region
C0006812biological_processmonoatomic cation transport
C0015267molecular_functionchannel activity
C0042151cellular_componentnematocyst
C0042802molecular_functionidentical protein binding
C0046930cellular_componentpore complex
C0046931biological_processpore complex assembly
C0051715biological_processcytolysis in another organism
C0055085biological_processtransmembrane transport
D0005576cellular_componentextracellular region
D0006812biological_processmonoatomic cation transport
D0015267molecular_functionchannel activity
D0042151cellular_componentnematocyst
D0042802molecular_functionidentical protein binding
D0046930cellular_componentpore complex
D0046931biological_processpore complex assembly
D0051715biological_processcytolysis in another organism
D0055085biological_processtransmembrane transport
E0005576cellular_componentextracellular region
E0006812biological_processmonoatomic cation transport
E0015267molecular_functionchannel activity
E0042151cellular_componentnematocyst
E0042802molecular_functionidentical protein binding
E0046930cellular_componentpore complex
E0046931biological_processpore complex assembly
E0051715biological_processcytolysis in another organism
E0055085biological_processtransmembrane transport
F0005576cellular_componentextracellular region
F0006812biological_processmonoatomic cation transport
F0015267molecular_functionchannel activity
F0042151cellular_componentnematocyst
F0042802molecular_functionidentical protein binding
F0046930cellular_componentpore complex
F0046931biological_processpore complex assembly
F0051715biological_processcytolysis in another organism
F0055085biological_processtransmembrane transport
G0005576cellular_componentextracellular region
G0006812biological_processmonoatomic cation transport
G0015267molecular_functionchannel activity
G0042151cellular_componentnematocyst
G0042802molecular_functionidentical protein binding
G0046930cellular_componentpore complex
G0046931biological_processpore complex assembly
G0051715biological_processcytolysis in another organism
G0055085biological_processtransmembrane transport
H0005576cellular_componentextracellular region
H0006812biological_processmonoatomic cation transport
H0015267molecular_functionchannel activity
H0042151cellular_componentnematocyst
H0042802molecular_functionidentical protein binding
H0046930cellular_componentpore complex
H0046931biological_processpore complex assembly
H0051715biological_processcytolysis in another organism
H0055085biological_processtransmembrane transport
I0005576cellular_componentextracellular region
I0006812biological_processmonoatomic cation transport
I0015267molecular_functionchannel activity
I0042151cellular_componentnematocyst
I0042802molecular_functionidentical protein binding
I0046930cellular_componentpore complex
I0046931biological_processpore complex assembly
I0051715biological_processcytolysis in another organism
I0055085biological_processtransmembrane transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues135
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 Residues18
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 Residues18
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 Residues27
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28630155","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues81
DetailsBinding site: {"description":"in monomeric and oligomeric forms","evidences":[{"source":"PubMed","id":"25716479","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues9
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 Residues9
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 Residues9
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 Residues9
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 Residues9
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

254917

PDB entries from 2026-06-10

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