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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6N4Q

CryoEM structure of Nav1.7 VSD2 (actived state) in complex with the gating modifier toxin ProTx2

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0005261molecular_functionmonoatomic cation channel activity
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0016020cellular_componentmembrane
A0055085biological_processtransmembrane transport
B0005216molecular_functionmonoatomic ion channel activity
B0005261molecular_functionmonoatomic cation channel activity
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0016020cellular_componentmembrane
B0055085biological_processtransmembrane transport
C0005216molecular_functionmonoatomic ion channel activity
C0005261molecular_functionmonoatomic cation channel activity
C0005886cellular_componentplasma membrane
C0006811biological_processmonoatomic ion transport
C0016020cellular_componentmembrane
C0055085biological_processtransmembrane transport
D0005216molecular_functionmonoatomic ion channel activity
D0005261molecular_functionmonoatomic cation channel activity
D0005886cellular_componentplasma membrane
D0006811biological_processmonoatomic ion transport
D0016020cellular_componentmembrane
D0055085biological_processtransmembrane transport
E0005246molecular_functioncalcium channel regulator activity
E0005576cellular_componentextracellular region
E0008289molecular_functionlipid binding
E0017080molecular_functionsodium channel regulator activity
E0035821biological_processmodulation of process of another organism
E0090729molecular_functiontoxin activity
E0099106molecular_functionion channel regulator activity
F0005246molecular_functioncalcium channel regulator activity
F0005576cellular_componentextracellular region
F0008289molecular_functionlipid binding
F0017080molecular_functionsodium channel regulator activity
F0035821biological_processmodulation of process of another organism
F0090729molecular_functiontoxin activity
F0099106molecular_functionion channel regulator activity
G0005246molecular_functioncalcium channel regulator activity
G0005576cellular_componentextracellular region
G0008289molecular_functionlipid binding
G0017080molecular_functionsodium channel regulator activity
G0035821biological_processmodulation of process of another organism
G0090729molecular_functiontoxin activity
G0099106molecular_functionion channel regulator activity
H0005246molecular_functioncalcium channel regulator activity
H0005576cellular_componentextracellular region
H0008289molecular_functionlipid binding
H0017080molecular_functionsodium channel regulator activity
H0035821biological_processmodulation of process of another organism
H0090729molecular_functiontoxin activity
H0099106molecular_functionion channel regulator activity
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
ITYR193-HIS199
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI7
Number of Residues64
DetailsTransmembrane: {"description":"Helical; Name=S1 of repeat II","evidences":[{"source":"PubMed","id":"30765606","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6J8I","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues108
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"30765606","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues96
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"30765606","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues64
DetailsTransmembrane: {"description":"Helical; Name=S3 of repeat II","evidences":[{"source":"PubMed","id":"30765606","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6J8I","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues64
DetailsTransmembrane: {"description":"Helical; Name=S4 of repeat II","evidences":[{"source":"PubMed","id":"30765606","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6J8I","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues88
DetailsTransmembrane: {"description":"Helical; Name=S5 of repeat II","evidences":[{"source":"PubMed","id":"30765606","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6J8I","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues104
DetailsTransmembrane: {"description":"Helical; Name=S6 of repeat II","evidences":[{"source":"PubMed","id":"30765606","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6J8I","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues8
DetailsSite: {"description":"Is directly targeted by the spider protoxin-II","evidences":[{"source":"PubMed","id":"30661758","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues116
DetailsPeptide: {"description":"Beta/omega-theraphotoxin-Tp2a","featureId":"PRO_0000044556","evidences":[{"source":"PubMed","id":"12475222","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues16
DetailsRegion: {"description":"Flexible tail region important for ability to inhibit Nav channel","evidences":[{"source":"PubMed","id":"25026046","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues4
DetailsRegion: {"description":"Hydrophobic dyad that anchors the toxin into the membrane while positioning it over the S3 helix of Nav1.7/SCN9A","evidences":[{"source":"PubMed","id":"30661758","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues12
DetailsSite: {"description":"Part of an aromatic-rich surface that anchors the toxin toward the membrane core relative to lipid headgroups bound along the pore module of Nav1.7/SCN9A","evidences":[{"source":"PubMed","id":"30661758","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues4
DetailsSite: {"description":"Electrostatic gating-modifier of Nav1.7/SCN9A that antagonizes outward gating-charge movement through direct electrostatic repulsion; may also indirectly antagonize S4 gating-charge movement by neutralizing acidic side chains within the extracellular vestibule of VSD2","evidences":[{"source":"PubMed","id":"30661758","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues4
DetailsSite: {"description":"Part of an aromatic-rich surface that anchors the toxin toward the membrane core relative to lipid headgroups bound along the pore module of Nav1.7/SCN9A; it also stabilizes the toxin for productive receptor site engagement","evidences":[{"source":"PubMed","id":"30661758","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues4
DetailsSite: {"description":"Antagonizes outward gating-charge movement of Nav1.7/SCN9A through direct electrostatic repulsion; may also indirectly antagonize S4 gating-charge movement by neutralizing acidic side chains within the extracellular vestibule of VSD2","evidences":[{"source":"PubMed","id":"30661758","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

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PDB entries from 2025-12-17

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