Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5GWF

FraC with GlcNAc(6S) bound

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
C0005576cellular_componentextracellular region
C0006811biological_processmonoatomic ion transport
C0006812biological_processmonoatomic cation transport
C0008289molecular_functionlipid binding
C0015267molecular_functionchannel activity
C0016020cellular_componentmembrane
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
C0046930cellular_componentpore complex
C0046931biological_processpore complex assembly
C0051715biological_processcytolysis in another organism
C0055085biological_processtransmembrane transport
C0090729molecular_functiontoxin activity
D0005576cellular_componentextracellular region
D0006811biological_processmonoatomic ion transport
D0006812biological_processmonoatomic cation transport
D0008289molecular_functionlipid binding
D0015267molecular_functionchannel activity
D0016020cellular_componentmembrane
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
D0046930cellular_componentpore complex
D0046931biological_processpore complex assembly
D0051715biological_processcytolysis in another organism
D0055085biological_processtransmembrane transport
D0090729molecular_functiontoxin activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: in subunit A; in oligomeric forms only => ECO:0000305|PubMed:25716479
ChainResidueDetails
AARG31
AGLY168
BARG31
BGLY168
CARG31
CGLY168
DARG31
DGLY168

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:28630155
ChainResidueDetails
ATYR51
DTYR51
DARG53
DTYR138
AARG53
ATYR138
BTYR51
BARG53
BTYR138
CTYR51
CARG53
CTYR138

site_idSWS_FT_FI3
Number of Residues36
DetailsBINDING: in monomeric and oligomeric forms => ECO:0000305|PubMed:25716479
ChainResidueDetails
ASER54
BSER54
BGLY85
BTYR108
BTYR113
BSER114
BTRP116
BTYR133
BTYR137
BARG144
CSER54
AGLY85
CGLY85
CTYR108
CTYR113
CSER114
CTRP116
CTYR133
CTYR137
CARG144
DSER54
DGLY85
ATYR108
DTYR108
DTYR113
DSER114
DTRP116
DTYR133
DTYR137
DARG144
ATYR113
ASER114
ATRP116
ATYR133
ATYR137
AARG144

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: in subunit B; in oligomeric forms only => ECO:0000305|PubMed:25716479
ChainResidueDetails
AARG79
BARG79
CARG79
DARG79

site_idSWS_FT_FI5
Number of Residues4
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
CPHE16
DPHE16

site_idSWS_FT_FI6
Number of Residues4
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
CVAL60
DVAL60

site_idSWS_FT_FI7
Number of Residues4
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
CTRP149
DTRP149

site_idSWS_FT_FI8
Number of Residues4
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
CPHE163
DPHE163

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon