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

7DTD

Voltage-gated sodium channel Nav1.1 and beta4

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
A0005654cellular_componentnucleoplasm
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006814biological_processsodium ion transport
A0007628biological_processadult walking behavior
A0008340biological_processdetermination of adult lifespan
A0014704cellular_componentintercalated disc
A0016020cellular_componentmembrane
A0016604cellular_componentnuclear body
A0019227biological_processneuronal action potential propagation
A0019228biological_processneuronal action potential
A0021675biological_processnerve development
A0030018cellular_componentZ disc
A0030315cellular_componentT-tubule
A0030424cellular_componentaxon
A0033268cellular_componentnode of Ranvier
A0034220biological_processmonoatomic ion transmembrane transport
A0034702cellular_componentmonoatomic ion channel complex
A0034706cellular_componentsodium channel complex
A0035725biological_processsodium ion transmembrane transport
A0042391biological_processregulation of membrane potential
A0043025cellular_componentneuronal cell body
A0043194cellular_componentaxon initial segment
A0050884biological_processneuromuscular process controlling posture
A0050966biological_processdetection of mechanical stimulus involved in sensory perception of pain
A0051649biological_processestablishment of localization in cell
A0055085biological_processtransmembrane transport
A0086002biological_processcardiac muscle cell action potential involved in contraction
A0086010biological_processmembrane depolarization during action potential
A0099505biological_processregulation of presynaptic membrane potential
A0099508molecular_functionvoltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential
B0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00648
Number of Residues15
DetailsRIBONUCLEASE_P Bacterial ribonuclease P protein component signature. IqrAyrRHLLKRtVK
ChainResidueDetails
AILE1922-LYS1936

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1103
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
AMET1-SER128
AGLY1480-VAL1542
ALYS1591-ILE1602
ALYS1651-ALA1669
ALEU1786-LYS2009
AARG176-PRO189
APRO231-ASP249
AVAL421-PRO768
AILE819-TRP832
ATRP873-GLY888
ALEU992-TRP1219
ALYS1270-ALA1283
APHE1330-SER1346

site_idSWS_FT_FI2
Number of Residues18
DetailsTRANSMEM: Helical; Name=S1 of repeat I => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ALEU129-MET147

site_idSWS_FT_FI3
Number of Residues323
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
ASER148-THR154
AALA1303-GLY1310
AASN1367-VAL1418
AALA1441-LEU1457
AGLU1561-THR1571
ALEU1621-THR1633
AGLY1688-THR1709
AILE1733-GLY1762
AASP208-SER213
AMET270-THR367
AARG393-TYR399
AGLU788-ASN798
AGLU853-GLY854
AGLY908-ASP936
AASP958-THR970
AGLU1238-THR1250

site_idSWS_FT_FI4
Number of Residues20
DetailsTRANSMEM: Helical; Name=S2 of repeat I => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ALYS155-ALA175
BASN71
BASN113

site_idSWS_FT_FI5
Number of Residues17
DetailsTRANSMEM: Helical; Name=S3 of repeat I => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ATRP190-VAL207

site_idSWS_FT_FI6
Number of Residues16
DetailsTRANSMEM: Helical; Name=S4 of repeat I => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AALA214-ILE230

site_idSWS_FT_FI7
Number of Residues19
DetailsTRANSMEM: Helical; Name=S5 of repeat I => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AVAL250-PHE269

site_idSWS_FT_FI8
Number of Residues87
DetailsINTRAMEM: Pore-forming => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
APHE368-LEU392
APHE937-TRP957
AGLY1419-ALA1440
APHE1710-PRO1732

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=S6 of repeat I => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AMET400-ALA420

site_idSWS_FT_FI10
Number of Residues18
DetailsTRANSMEM: Helical; Name=S1 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
APHE769-MET787

site_idSWS_FT_FI11
Number of Residues19
DetailsTRANSMEM: Helical; Name=S2 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AVAL799-LYS818

site_idSWS_FT_FI12
Number of Residues19
DetailsTRANSMEM: Helical; Name=S3 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AASN833-VAL852

site_idSWS_FT_FI13
Number of Residues17
DetailsTRANSMEM: Helical; Name=S4 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ALEU855-SER872

site_idSWS_FT_FI14
Number of Residues18
DetailsTRANSMEM: Helical; Name=S5 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AALA889-VAL907

site_idSWS_FT_FI15
Number of Residues20
DetailsTRANSMEM: Helical; Name=S6 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AVAL971-LEU991

site_idSWS_FT_FI16
Number of Residues17
DetailsTRANSMEM: Helical; Name=S1 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
APHE1220-PHE1237

site_idSWS_FT_FI17
Number of Residues18
DetailsTRANSMEM: Helical; Name=S2 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AMET1251-LEU1269

site_idSWS_FT_FI18
Number of Residues18
DetailsTRANSMEM: Helical; Name=S3 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ATRP1284-ASN1302

site_idSWS_FT_FI19
Number of Residues18
DetailsTRANSMEM: Helical; Name=S4 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AALA1311-ARG1329

site_idSWS_FT_FI20
Number of Residues19
DetailsTRANSMEM: Helical; Name=S5 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AILE1347-VAL1366

site_idSWS_FT_FI21
Number of Residues21
DetailsTRANSMEM: Helical; Name=S6 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ATYR1458-ILE1479

site_idSWS_FT_FI22
Number of Residues17
DetailsTRANSMEM: Helical; Name=S1 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
APHE1543-VAL1560

site_idSWS_FT_FI23
Number of Residues18
DetailsTRANSMEM: Helical; Name=S2 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AILE1572-LEU1590

site_idSWS_FT_FI24
Number of Residues17
DetailsTRANSMEM: Helical; Name=S3 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AGLY1603-PHE1620

site_idSWS_FT_FI25
Number of Residues16
DetailsTRANSMEM: Helical; Name=S4 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ALEU1634-ILE1650

site_idSWS_FT_FI26
Number of Residues17
DetailsTRANSMEM: Helical; Name=S5 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ALEU1670-PHE1687

site_idSWS_FT_FI27
Number of Residues22
DetailsTRANSMEM: Helical; Name=S6 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AILE1763-ILE1785

site_idSWS_FT_FI28
Number of Residues1
DetailsSITE: Key residue that permits the spider beta/delta-theraphotoxin-Pre1a to inhibit fast inactivation of the channel => ECO:0000269|PubMed:28428547
ChainResidueDetails
ASER1574

site_idSWS_FT_FI29
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04774
ChainResidueDetails
ASER470
ASER523
ASER525
ASER550
ASER607
ASER730

site_idSWS_FT_FI30
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:A2APX8
ChainResidueDetails
ASER551

site_idSWS_FT_FI31
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000250|UniProtKB:P04775
ChainResidueDetails
ASER1516

site_idSWS_FT_FI32
Number of Residues9
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN211
AASN284
AASN295
AASN301
AASN306
AASN338
AASN1378
AASN1392
AASN1403

225158

PDB entries from 2024-09-18

PDB statisticsPDBj update infoContact PDBjnumon