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6J8G

Structure of human voltage-gated sodium channel Nav1.7 in complex with auxiliary beta subunits, huwentoxin-IV and saxitoxin (Y1755 up)

Functional Information from GO Data
ChainGOidnamespacecontents
A0001518cellular_componentvoltage-gated sodium channel complex
A0005216molecular_functionmonoatomic ion channel activity
A0005248molecular_functionvoltage-gated sodium channel activity
A0005261molecular_functionmonoatomic cation channel activity
A0005272molecular_functionsodium channel activity
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006814biological_processsodium ion transport
A0006954biological_processinflammatory response
A0007623biological_processcircadian rhythm
A0009636biological_processresponse to toxic substance
A0009791biological_processpost-embryonic development
A0016020cellular_componentmembrane
A0019228biological_processneuronal action potential
A0019233biological_processsensory perception of pain
A0030424cellular_componentaxon
A0033268cellular_componentnode of Ranvier
A0034220biological_processmonoatomic ion transmembrane transport
A0034702cellular_componentmonoatomic ion channel complex
A0035725biological_processsodium ion transmembrane transport
A0042995cellular_componentcell projection
A0043679cellular_componentaxon terminus
A0048266biological_processbehavioral response to pain
A0050965biological_processdetection of temperature stimulus involved in sensory perception of pain
A0050974biological_processdetection of mechanical stimulus involved in sensory perception
A0055085biological_processtransmembrane transport
A0086002biological_processcardiac muscle cell action potential involved in contraction
A0098870biological_processaction potential propagation
B0001518cellular_componentvoltage-gated sodium channel complex
B0006814biological_processsodium ion transport
B0017080molecular_functionsodium channel regulator activity
C0016020cellular_componentmembrane
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues138
DetailsTOPO_DOM: Extracellular => ECO:0000305|PubMed:30190309
ChainResidueDetails
BGLY19-ILE157
AGLY1454-ALA1516
ALYS1565-VAL1576
ALYS1625-ALA1643
ALEU1760-LYS1988
AARG174-PRO187
APRO229-ASP247
AVAL400-PRO744
ALEU795-TRP808
ATRP849-GLY864
ALEU968-TRP1193
ALYS1244-ALA1257
APHE1304-SER1320

site_idSWS_FT_FI2
Number of Residues21
DetailsTRANSMEM: Helical => ECO:0000305|PubMed:30190309, ECO:0007744|PDB:6AGF
ChainResidueDetails
BVAL158-ILE179

site_idSWS_FT_FI3
Number of Residues38
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:30190309
ChainResidueDetails
BTYR180-GLU218
ATHR1277-GLY1284
AASN1341-VAL1392
AALA1415-LEU1431
AGLU1535-GLU1545
ALEU1595-THR1607
AGLY1662-THR1683
AILE1707-GLY1736
AASN206-SER211
AMET268-THR346
AARG372-TYR378
AGLU764-ASN774
AGLU829-GLY830
AGLY884-ASP912
AASP934-ILE946
AGLU1212-ILE1224

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:30765606, ECO:0000269|PubMed:36696443, ECO:0007744|PDB:6J8G, ECO:0007744|PDB:6J8H, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:6J8J, ECO:0007744|PDB:8FHD
ChainResidueDetails
BASN93
CARG135

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:30190309, ECO:0000269|PubMed:30765606, ECO:0000269|PubMed:36696443, ECO:0007744|PDB:6AGF, ECO:0007744|PDB:6J8G, ECO:0007744|PDB:6J8H, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:6J8J, ECO:0007744|PDB:8FHD
ChainResidueDetails
BASN110
BASN114

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:30765606, ECO:0000269|PubMed:36696443, ECO:0000269|PubMed:36823201, ECO:0007744|PDB:6J8G, ECO:0007744|PDB:6J8H, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:6J8J, ECO:0007744|PDB:8FHD, ECO:0007744|PDB:8GZ1, ECO:0007744|PDB:8GZ2
ChainResidueDetails
BASN135

site_idSWS_FT_FI7
Number of Residues19
DetailsTRANSMEM: Helical; Name=S5 of repeat I => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AVAL248-PHE267
CASN74

site_idSWS_FT_FI8
Number of Residues87
DetailsINTRAMEM: Pore-forming => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
APHE347-LEU371
APHE913-TRP933
AGLY1393-ALA1414
APHE1684-PRO1706

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=S6 of repeat I => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AMET379-ALA399

site_idSWS_FT_FI10
Number of Residues18
DetailsTRANSMEM: Helical; Name=S1 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
APHE745-MET763

site_idSWS_FT_FI11
Number of Residues19
DetailsTRANSMEM: Helical; Name=S2 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AVAL775-LYS794

site_idSWS_FT_FI12
Number of Residues19
DetailsTRANSMEM: Helical; Name=S3 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AASN809-VAL828

site_idSWS_FT_FI13
Number of Residues17
DetailsTRANSMEM: Helical; Name=S4 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ALEU831-SER848

site_idSWS_FT_FI14
Number of Residues18
DetailsTRANSMEM: Helical; Name=S5 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AALA865-VAL883

site_idSWS_FT_FI15
Number of Residues20
DetailsTRANSMEM: Helical; Name=S6 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AVAL947-LEU967

site_idSWS_FT_FI16
Number of Residues17
DetailsTRANSMEM: Helical; Name=S1 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
APHE1194-PHE1211

site_idSWS_FT_FI17
Number of Residues18
DetailsTRANSMEM: Helical; Name=S2 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AILE1225-LEU1243

site_idSWS_FT_FI18
Number of Residues18
DetailsTRANSMEM: Helical; Name=S3 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ATRP1258-ASN1276

site_idSWS_FT_FI19
Number of Residues18
DetailsTRANSMEM: Helical; Name=S4 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
APRO1285-ARG1303

site_idSWS_FT_FI20
Number of Residues19
DetailsTRANSMEM: Helical; Name=S5 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AILE1321-VAL1340

site_idSWS_FT_FI21
Number of Residues21
DetailsTRANSMEM: Helical; Name=S6 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ATYR1432-ILE1453

site_idSWS_FT_FI22
Number of Residues17
DetailsTRANSMEM: Helical; Name=S1 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
APHE1517-VAL1534

site_idSWS_FT_FI23
Number of Residues18
DetailsTRANSMEM: Helical; Name=S2 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AVAL1546-LEU1564

site_idSWS_FT_FI24
Number of Residues17
DetailsTRANSMEM: Helical; Name=S3 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AGLY1577-PHE1594

site_idSWS_FT_FI25
Number of Residues16
DetailsTRANSMEM: Helical; Name=S4 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ALEU1608-VAL1624

site_idSWS_FT_FI26
Number of Residues17
DetailsTRANSMEM: Helical; Name=S5 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ALEU1644-PHE1661

site_idSWS_FT_FI27
Number of Residues22
DetailsTRANSMEM: Helical; Name=S6 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AILE1737-ILE1759

site_idSWS_FT_FI28
Number of Residues2
DetailsSITE: Is directly targeted by the spider protoxin-II => ECO:0000269|PubMed:30661758
ChainResidueDetails
AGLU822
AASP827

site_idSWS_FT_FI29
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:25240195
ChainResidueDetails
ASER1490

site_idSWS_FT_FI30
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN209

site_idSWS_FT_FI31
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:30765606, ECO:0007744|PDB:6J8G, ECO:0007744|PDB:6J8H, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:6J8J
ChainResidueDetails
AASN283
AASN1352
AASN1366
AASN1375

227561

PDB entries from 2024-11-20

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