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1O72

Crystal structure of the water-soluble state of the pore-forming cytolysin Sticholysin II complexed with phosphorylcholine

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0006811biological_processmonoatomic ion transport
A0006812biological_processmonoatomic cation transport
A0015267molecular_functionchannel activity
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
A0046930cellular_componentpore complex
A0046931biological_processpore complex assembly
A0051715biological_processcytolysis in another organism
A0055085biological_processtransmembrane transport
A0090729molecular_functiontoxin activity
B0005576cellular_componentextracellular region
B0006811biological_processmonoatomic ion transport
B0006812biological_processmonoatomic cation transport
B0015267molecular_functionchannel activity
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
B0046930cellular_componentpore complex
B0046931biological_processpore complex assembly
B0051715biological_processcytolysis in another organism
B0055085biological_processtransmembrane transport
B0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PC A1176
ChainResidue
ATYR111
ATYR136

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PC B1176
ChainResidue
BTYR111
BTYR131
BTYR135
BTYR136
BHOH2046

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsRegion: {"description":"Plays an important role in the hemolytic activity","evidences":[{"source":"PubMed","id":"16170802","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues38
DetailsRegion: {"description":"N-terminal region","evidences":[{"source":"UniProtKB","id":"P61914","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues30
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_FI4
Number of Residues4
DetailsMotif: {"description":"Cell attachment site, crucial for protein stability","evidences":[{"source":"PubMed","id":"24418371","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14604522","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsSite: {"description":"Important in the initial contact with the lipid membrane","evidences":[{"source":"UniProtKB","id":"P61914","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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