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1O71

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0006811biological_processmonoatomic ion transport
A0006812biological_processmonoatomic cation transport
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
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 PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A1176
ChainResidue
ATYR111
ATYR136

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A1177
ChainResidue
AARG29
AHOH2011
AHOH2072

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A1178
ChainResidue
APHE106
AASP107
ASER52
ATHR82
AGLY83
APRO105

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL B1176
ChainResidue
BTYR111
BTYR136

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B1177
ChainResidue
BSER28
BARG29
BPHE106
BHOH2067
BHOH2068
BHOH2069
BHOH2070

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B1178
ChainResidue
BSER52
BALA81
BTHR82
BGLY83
BPRO105
BPHE106
BASP107

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:14604522
ChainResidueDetails
ASER52
BSER103
BPRO105
BTYR131
BTYR135
BTYR136
AVAL85
ASER103
APRO105
ATYR131
ATYR135
ATYR136
BSER52
BVAL85

site_idSWS_FT_FI2
Number of Residues4
DetailsSITE: Important in the initial contact with the lipid membrane => ECO:0000250|UniProtKB:P61914
ChainResidueDetails
ATRP110
ATYR111
BTRP110
BTYR111

218853

PDB entries from 2024-04-24

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