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6K2G

Structure of FraE in the monomer state

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0006811biological_processmonoatomic ion transport
A0006812biological_processmonoatomic cation transport
A0008289molecular_functionlipid binding
A0015267molecular_functionchannel activity
A0016020cellular_componentmembrane
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
B0008289molecular_functionlipid binding
B0015267molecular_functionchannel activity
B0016020cellular_componentmembrane
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 SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: in subunit A; in oligomeric forms only => ECO:0000305|PubMed:25716479
ChainResidueDetails
AARG31
AGLY168
BARG31
BGLY168

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:28630155
ChainResidueDetails
ATYR51
AARG53
ATYR138
BTYR51
BARG53
BTYR138

site_idSWS_FT_FI3
Number of Residues18
DetailsBINDING: in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479
ChainResidueDetails
ASER54
BSER54
BGLY85
BTYR108
BTYR113
BSER114
BTRP116
BTYR133
BTYR137
BARG144
AGLY85
ATYR108
ATYR113
ASER114
ATRP116
ATYR133
ATYR137
AARG144

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: in subunit B; in oligomeric forms only => ECO:0000305|PubMed:25716479
ChainResidueDetails
AARG79
BARG79

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: 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
ChainResidueDetails
APHE16
BPHE16

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Protrudes from one subunit (B) and inserts into the hydrophobic cavity from the adjacent subunit (A) => ECO:0000305|PubMed:21300287, ECO:0000305|PubMed:25716479
ChainResidueDetails
AVAL60
BVAL60

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: 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
ChainResidueDetails
ATRP149
BTRP149

site_idSWS_FT_FI8
Number of Residues2
DetailsSITE: Part of the hydrophobic cavity (in subunit A) that receives Val-60 from the adjacent subunit (B) => ECO:0000305|PubMed:21300287
ChainResidueDetails
APHE163
BPHE163

226707

PDB entries from 2024-10-30

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