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

6AGF

Structure of the human voltage-gated sodium channel Nav1.4 in complex with beta1

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
A0006936biological_processmuscle contraction
A0016020cellular_componentmembrane
A0034220biological_processmonoatomic ion transmembrane transport
A0034702cellular_componentmonoatomic ion channel complex
A0035725biological_processsodium ion transmembrane transport
A0055085biological_processtransmembrane transport
A0086002biological_processcardiac muscle cell action potential involved in contraction
A0100001biological_processregulation of skeletal muscle contraction by action potential
B0001518cellular_componentvoltage-gated sodium channel complex
B0006814biological_processsodium ion transport
B0017080molecular_functionsodium channel regulator activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues141
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:30190309
ChainResidueDetails
BGLY19-GLU160
AGLY1292-ALA1354
ALYS1403-VAL1414
AARG1463-ALA1481
ALEU1598-VAL1836
AARG179-PRO192
APRO234-ASP252
AVAL445-PRO578
ALEU629-TRP642
ATRP683-GLY698
ALEU798-TRP1032
ALYS1083-ALA1096
APHE1143-SER1159

site_idSWS_FT_FI2
Number of Residues21
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:30190309
ChainResidueDetails
BILE161-TYR182

site_idSWS_FT_FI3
Number of Residues35
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:30190309
ChainResidueDetails
BLYS183-GLU218
ATRP1116-GLY1123
AASN1180-VAL1230
AALA1253-LEU1269
AGLU1373-ASP1383
ALEU1433-THR1445
AGLY1500-THR1521
AILE1545-GLY1574
AASP211-SER216
AMET273-THR391
AARG417-TYR423
AGLU598-ASN608
AGLN663-GLY664
AGLY718-ASP746
AASP768-CYS778
AGLU1051-THR1063

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

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:0000269|PubMed:30190309
ChainResidueDetails
AVAL253-PHE272

site_idSWS_FT_FI8
Number of Residues87
DetailsINTRAMEM: Pore-forming => ECO:0000269|PubMed:30190309
ChainResidueDetails
APHE392-LEU416
APHE747-TRP767
AGLY1231-ALA1252
APHE1522-PRO1544

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=S6 of repeat I => ECO:0000269|PubMed:30190309
ChainResidueDetails
AMET424-ALA444

site_idSWS_FT_FI10
Number of Residues18
DetailsTRANSMEM: Helical; Name=S1 of repeat II => ECO:0000269|PubMed:30190309
ChainResidueDetails
APHE579-MET597

site_idSWS_FT_FI11
Number of Residues19
DetailsTRANSMEM: Helical; Name=S2 of repeat II => ECO:0000269|PubMed:30190309
ChainResidueDetails
AVAL609-LYS628

site_idSWS_FT_FI12
Number of Residues19
DetailsTRANSMEM: Helical; Name=S3 of repeat II => ECO:0000269|PubMed:30190309
ChainResidueDetails
AASN643-VAL662

site_idSWS_FT_FI13
Number of Residues17
DetailsTRANSMEM: Helical; Name=S4 of repeat II => ECO:0000269|PubMed:30190309
ChainResidueDetails
ALEU665-SER682

site_idSWS_FT_FI14
Number of Residues18
DetailsTRANSMEM: Helical; Name=S5 of repeat II => ECO:0000269|PubMed:30190309
ChainResidueDetails
AALA699-VAL717

site_idSWS_FT_FI15
Number of Residues18
DetailsTRANSMEM: Helical; Name=S6 of repeat II => ECO:0000269|PubMed:30190309
ChainResidueDetails
ALEU779-PHE797

site_idSWS_FT_FI16
Number of Residues17
DetailsTRANSMEM: Helical; Name=S1 of repeat III => ECO:0000269|PubMed:30190309
ChainResidueDetails
APHE1033-PHE1050

site_idSWS_FT_FI17
Number of Residues18
DetailsTRANSMEM: Helical; Name=S2 of repeat III => ECO:0000269|PubMed:30190309
ChainResidueDetails
AILE1064-LEU1082

site_idSWS_FT_FI18
Number of Residues18
DetailsTRANSMEM: Helical; Name=S3 of repeat III => ECO:0000269|PubMed:30190309
ChainResidueDetails
ATRP1097-ASN1115

site_idSWS_FT_FI19
Number of Residues18
DetailsTRANSMEM: Helical; Name=S4 of repeat III => ECO:0000269|PubMed:30190309
ChainResidueDetails
APRO1124-ARG1142

site_idSWS_FT_FI20
Number of Residues19
DetailsTRANSMEM: Helical; Name=S5 of repeat III => ECO:0000269|PubMed:30190309
ChainResidueDetails
AILE1160-VAL1179

site_idSWS_FT_FI21
Number of Residues21
DetailsTRANSMEM: Helical; Name=S6 of repeat III => ECO:0000269|PubMed:30190309
ChainResidueDetails
ATYR1270-ILE1291

site_idSWS_FT_FI22
Number of Residues17
DetailsTRANSMEM: Helical; Name=S1 of repeat IV => ECO:0000269|PubMed:30190309
ChainResidueDetails
APHE1355-VAL1372

site_idSWS_FT_FI23
Number of Residues18
DetailsTRANSMEM: Helical; Name=S2 of repeat IV => ECO:0000269|PubMed:30190309
ChainResidueDetails
AILE1384-LEU1402

site_idSWS_FT_FI24
Number of Residues17
DetailsTRANSMEM: Helical; Name=S3 of repeat IV => ECO:0000269|PubMed:30190309
ChainResidueDetails
AGLY1415-ALA1432

site_idSWS_FT_FI25
Number of Residues16
DetailsTRANSMEM: Helical; Name=S4 of repeat IV => ECO:0000269|PubMed:30190309
ChainResidueDetails
ALEU1446-ILE1462

site_idSWS_FT_FI26
Number of Residues17
DetailsTRANSMEM: Helical; Name=S5 of repeat IV => ECO:0000269|PubMed:30190309
ChainResidueDetails
ALEU1482-PHE1499

site_idSWS_FT_FI27
Number of Residues22
DetailsTRANSMEM: Helical; Name=S6 of repeat IV => ECO:0000269|PubMed:30190309
ChainResidueDetails
AILE1575-ILE1597

site_idSWS_FT_FI28
Number of Residues1
DetailsSITE: Important for inhibition by tetrodotoxin => ECO:0000250|UniProtKB:P15390
ChainResidueDetails
ATYR407

site_idSWS_FT_FI29
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000250
ChainResidueDetails
ASER1328

site_idSWS_FT_FI30
Number of Residues9
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN214
AASN288
AASN291
AASN297
AASN303
AASN315
AASN321
AASN333
AASN1191

site_idSWS_FT_FI31
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:30190309, ECO:0007744|PDB:6AGF
ChainResidueDetails
AASN362
AASN1205

221371

PDB entries from 2024-06-19

PDB statisticsPDBj update infoContact PDBjnumon