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8FHD

Cryo-EM structure of human voltage-gated sodium channel Nav1.6

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
A0005524molecular_functionATP binding
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006814biological_processsodium ion transport
A0007399biological_processnervous system development
A0007422biological_processperipheral nervous system development
A0016020cellular_componentmembrane
A0019228biological_processneuronal action potential
A0021554biological_processoptic nerve development
A0030018cellular_componentZ disc
A0030054cellular_componentcell junction
A0030424cellular_componentaxon
A0031402molecular_functionsodium ion binding
A0031410cellular_componentcytoplasmic vesicle
A0033268cellular_componentnode of Ranvier
A0034220biological_processmonoatomic ion transmembrane transport
A0034702cellular_componentmonoatomic ion channel complex
A0035725biological_processsodium ion transmembrane transport
A0042552biological_processmyelination
A0042995cellular_componentcell projection
A0043194cellular_componentaxon initial segment
A0048787cellular_componentpresynaptic active zone membrane
A0055085biological_processtransmembrane transport
A0086002biological_processcardiac muscle cell action potential involved in contraction
A0098688cellular_componentparallel fiber to Purkinje cell synapse
A0098839cellular_componentpostsynaptic density membrane
A0098978cellular_componentglutamatergic synapse
C0001518cellular_componentvoltage-gated sodium channel complex
C0006814biological_processsodium ion transport
C0017080molecular_functionsodium channel regulator activity
Functional Information from PROSITE/UniProt
site_idPS00878
Number of Residues19
DetailsODR_DC_2_1 Orn/DAP/Arg decarboxylases family 2 pyridoxal-P attachment site. YAdKVFtyifILemLlkwT
ChainResidueDetails
ATYR1234-THR1252

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues141
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:30190309
ChainResidueDetails
CGLY19-GLU160
AGLY1461-ALA1523
ALYS1572-ILE1583
ALYS1632-ALA1650
ALEU1766-CYS1980
AARG180-PRO193
APRO235-ASP253
AVAL409-PRO753
ALEU804-TRP817
ATRP858-GLY873
ALEU977-TRP1199
ALYS1250-ALA1263
APHE1310-SER1326

site_idSWS_FT_FI2
Number of Residues21
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:30190309
ChainResidueDetails
CILE161-TYR182

site_idSWS_FT_FI3
Number of Residues35
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:30190309
ChainResidueDetails
CLYS183-GLU218
AALA1283-GLY1290
AASN1347-VAL1399
AALA1422-ILE1438
AGLU1542-ASN1552
ALEU1602-THR1614
AGLY1669-THR1690
AILE1714-GLY1742
AASN212-SER217
AMET274-THR355
AARG381-TYR387
AGLU773-HIS783
AGLU838-GLY839
AGLY893-ASP921
AASP943-ILE955
AGLU1218-THR1230

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
CASN93

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
CASN110
CASN114

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
CASN135

site_idSWS_FT_FI7
Number of Residues19
DetailsTRANSMEM: Helical; Name=S5 of repeat I => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AVAL254-PHE273

site_idSWS_FT_FI8
Number of Residues87
DetailsINTRAMEM: Pore-forming => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
APHE356-LEU380
APHE922-TRP942
AGLY1400-ALA1421
APHE1691-PRO1713

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=S6 of repeat I => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AMET388-ALA408

site_idSWS_FT_FI10
Number of Residues18
DetailsTRANSMEM: Helical; Name=S1 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
APHE754-MET772

site_idSWS_FT_FI11
Number of Residues19
DetailsTRANSMEM: Helical; Name=S2 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AVAL784-LYS803

site_idSWS_FT_FI12
Number of Residues19
DetailsTRANSMEM: Helical; Name=S3 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AASN818-VAL837

site_idSWS_FT_FI13
Number of Residues17
DetailsTRANSMEM: Helical; Name=S4 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ALEU840-SER857

site_idSWS_FT_FI14
Number of Residues18
DetailsTRANSMEM: Helical; Name=S5 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AALA874-VAL892

site_idSWS_FT_FI15
Number of Residues20
DetailsTRANSMEM: Helical; Name=S6 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AVAL956-LEU976

site_idSWS_FT_FI16
Number of Residues17
DetailsTRANSMEM: Helical; Name=S1 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
APHE1200-PHE1217

site_idSWS_FT_FI17
Number of Residues18
DetailsTRANSMEM: Helical; Name=S2 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AILE1231-LEU1249

site_idSWS_FT_FI18
Number of Residues18
DetailsTRANSMEM: Helical; Name=S3 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ATRP1264-ASN1282

site_idSWS_FT_FI19
Number of Residues18
DetailsTRANSMEM: Helical; Name=S4 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AALA1291-ARG1309

site_idSWS_FT_FI20
Number of Residues19
DetailsTRANSMEM: Helical; Name=S5 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AILE1327-VAL1346

site_idSWS_FT_FI21
Number of Residues21
DetailsTRANSMEM: Helical; Name=S6 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ATYR1439-ILE1460

site_idSWS_FT_FI22
Number of Residues17
DetailsTRANSMEM: Helical; Name=S1 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
APHE1524-VAL1541

site_idSWS_FT_FI23
Number of Residues18
DetailsTRANSMEM: Helical; Name=S2 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AILE1553-LEU1571

site_idSWS_FT_FI24
Number of Residues17
DetailsTRANSMEM: Helical; Name=S3 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AGLY1584-PHE1601

site_idSWS_FT_FI25
Number of Residues16
DetailsTRANSMEM: Helical; Name=S4 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ALEU1615-ILE1631

site_idSWS_FT_FI26
Number of Residues17
DetailsTRANSMEM: Helical; Name=S5 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ALEU1651-PHE1668

site_idSWS_FT_FI27
Number of Residues22
DetailsTRANSMEM: Helical; Name=S6 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AILE1743-ILE1765

site_idSWS_FT_FI28
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:36823201, ECO:0007744|PDB:8GZ1
ChainResidueDetails
ATYR371
AGLU373
AGLU939
ALYS1413

site_idSWS_FT_FI29
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AGLY893

site_idSWS_FT_FI30
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O88420
ChainResidueDetails
ASER518
ASER520

site_idSWS_FT_FI31
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000250|UniProtKB:Q15858
ChainResidueDetails
ASER1497

site_idSWS_FT_FI32
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN215
AASN1383

site_idSWS_FT_FI33
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:36823201, ECO:0007744|PDB:8GZ1, ECO:0007744|PDB:8GZ2
ChainResidueDetails
AASN289

site_idSWS_FT_FI34
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:36696443, ECO:0000269|PubMed:36823201, ECO:0000312|PDB:8FHD, ECO:0007744|PDB:8GZ1, ECO:0007744|PDB:8GZ2
ChainResidueDetails
AASN295
AASN308
AASN1358
AASN1372

site_idSWS_FT_FI35
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:36696443, ECO:0000269|PubMed:36823201, ECO:0007744|PDB:8FHD, ECO:0007744|PDB:8GZ1, ECO:0007744|PDB:8GZ2
ChainResidueDetails
AASN326

221716

PDB entries from 2024-06-26

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