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8F0P

Structure of VSD4-NaV1.7-NaVPas channel chimera bound to the hybrid inhibitor GNE-1305

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
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006814biological_processsodium ion transport
A0016020cellular_componentmembrane
A0055085biological_processtransmembrane transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues590
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:28183995, ECO:0007744|PDB:5X0M
ChainResidueDetails
AMET1-PRO140
AARG187-PRO200
APRO242-ASP260
AVAL414-PRO519
AILE570-TRP583
ATRP624-GLY639
ALEU741-TYR857
AMET908-LYS921
AVAL965-HIS981
ALEU1411-ASN1553

site_idSWS_FT_FI2
Number of Residues18
DetailsTRANSMEM: Helical; Name=S1 of repeat I => ECO:0000269|PubMed:28183995, ECO:0007744|PDB:5X0M
ChainResidueDetails
AILE141-MET159

site_idSWS_FT_FI3
Number of Residues267
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:28183995, ECO:0007744|PDB:5X0M
ChainResidueDetails
APRO160-THR165
AASP219-TYR224
AMET281-THR360
AARG386-HIS392
AASP539-ARG549
AGLN604-GLY605
AGLY659-ASP686
AASP708-PRO719
AGLU876-ASN888
ACYS941-GLU945
AGLN1002-VAL1047
AALA1070-ILE1086
AGLY1317-THR1338
AILE1362-GLY1387

site_idSWS_FT_FI4
Number of Residues20
DetailsTRANSMEM: Helical; Name=S2 of repeat I => ECO:0000269|PubMed:28183995, ECO:0007744|PDB:5X0M
ChainResidueDetails
ATYR166-ALA186

site_idSWS_FT_FI5
Number of Residues17
DetailsTRANSMEM: Helical; Name=S3 of repeat I => ECO:0000269|PubMed:28183995, ECO:0007744|PDB:5X0M
ChainResidueDetails
ATRP201-VAL218

site_idSWS_FT_FI6
Number of Residues16
DetailsTRANSMEM: Helical; Name=S4 of repeat I => ECO:0000269|PubMed:28183995, ECO:0007744|PDB:5X0M
ChainResidueDetails
AALA225-VAL241

site_idSWS_FT_FI7
Number of Residues19
DetailsTRANSMEM: Helical; Name=S5 of repeat I => ECO:0000269|PubMed:28183995, ECO:0007744|PDB:5X0M
ChainResidueDetails
ALEU261-PHE280

site_idSWS_FT_FI8
Number of Residues87
DetailsINTRAMEM: Pore-forming => ECO:0000269|PubMed:28183995, ECO:0007744|PDB:5X0M
ChainResidueDetails
APHE361-LEU385
APHE687-TRP707
AGLY1048-ASP1069
APHE1339-ALA1361

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=S6 of repeat I => ECO:0000269|PubMed:28183995, ECO:0007744|PDB:5X0M
ChainResidueDetails
AILE393-ALA413

site_idSWS_FT_FI10
Number of Residues18
DetailsTRANSMEM: Helical; Name=S1 of repeat II => ECO:0000269|PubMed:28183995, ECO:0007744|PDB:5X0M
ChainResidueDetails
APHE520-LEU538

site_idSWS_FT_FI11
Number of Residues19
DetailsTRANSMEM: Helical; Name=S2 of repeat II => ECO:0000269|PubMed:28183995, ECO:0007744|PDB:5X0M
ChainResidueDetails
AILE550-LYS569

site_idSWS_FT_FI12
Number of Residues19
DetailsTRANSMEM: Helical; Name=S3 of repeat II => ECO:0000269|PubMed:28183995, ECO:0007744|PDB:5X0M
ChainResidueDetails
AASN584-VAL603

site_idSWS_FT_FI13
Number of Residues17
DetailsTRANSMEM: Helical; Name=S4 of repeat II => ECO:0000269|PubMed:28183995, ECO:0007744|PDB:5X0M
ChainResidueDetails
ALEU606-PHE623

site_idSWS_FT_FI14
Number of Residues18
DetailsTRANSMEM: Helical; Name=S5 of repeat II => ECO:0000269|PubMed:28183995, ECO:0007744|PDB:5X0M
ChainResidueDetails
AALA640-ILE658

site_idSWS_FT_FI15
Number of Residues20
DetailsTRANSMEM: Helical; Name=S6 of repeat II => ECO:0000269|PubMed:28183995, ECO:0007744|PDB:5X0M
ChainResidueDetails
APHE720-LEU740

site_idSWS_FT_FI16
Number of Residues17
DetailsTRANSMEM: Helical; Name=S1 of repeat III => ECO:0000269|PubMed:28183995, ECO:0007744|PDB:5X0M
ChainResidueDetails
APHE858-LEU875

site_idSWS_FT_FI17
Number of Residues18
DetailsTRANSMEM: Helical; Name=S2 of repeat III => ECO:0000269|PubMed:28183995, ECO:0007744|PDB:5X0M
ChainResidueDetails
AILE889-ILE907

site_idSWS_FT_FI18
Number of Residues18
DetailsTRANSMEM: Helical; Name=S3 of repeat III => ECO:0000269|PubMed:28183995, ECO:0007744|PDB:5X0M
ChainResidueDetails
ATRP922-MET940

site_idSWS_FT_FI19
Number of Residues18
DetailsTRANSMEM: Helical; Name=S4 of repeat III => ECO:0000269|PubMed:28183995, ECO:0007744|PDB:5X0M
ChainResidueDetails
AALA946-LYS964

site_idSWS_FT_FI20
Number of Residues19
DetailsTRANSMEM: Helical; Name=S5 of repeat III => ECO:0000269|PubMed:28183995, ECO:0007744|PDB:5X0M
ChainResidueDetails
AILE982-VAL1001

site_idSWS_FT_FI21
Number of Residues21
DetailsTRANSMEM: Helical; Name=S6 of repeat III => ECO:0000269|PubMed:28183995, ECO:0007744|PDB:5X0M
ChainResidueDetails
ATYR1087-VAL1108

site_idSWS_FT_FI22
Number of Residues17
DetailsTRANSMEM: Helical; Name=S5 of repeat IV => ECO:0000269|PubMed:28183995, ECO:0007744|PDB:5X0M
ChainResidueDetails
ALEU1299-PHE1316

site_idSWS_FT_FI23
Number of Residues22
DetailsTRANSMEM: Helical; Name=S6 of repeat IV => ECO:0000269|PubMed:28183995, ECO:0007744|PDB:5X0M
ChainResidueDetails
AILE1388-ILE1410

site_idSWS_FT_FI24
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:30049784, ECO:0007744|PDB:6A91
ChainResidueDetails
AGLU378
ATRP1063

site_idSWS_FT_FI25
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:30049784, ECO:0007744|PDB:6A95
ChainResidueDetails
AGLU701
AGLU704
AGLY1062
AGLY1354
AASP1356

site_idSWS_FT_FI26
Number of Residues7
DetailsSITE: Interacts with the spider Mu-diguetoxin-Dc1a => ECO:0000269|PubMed:30049784
ChainResidueDetails
AASP539
AASP542
AARG549
AARG613
AGLN1002
AARG1027
AHIS1032

site_idSWS_FT_FI27
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:28183995, ECO:0007744|PDB:5X0M
ChainResidueDetails
AASN300

site_idSWS_FT_FI28
Number of Residues5
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:28183995, ECO:0000269|PubMed:30049784, ECO:0007744|PDB:5X0M, ECO:0007744|PDB:6A90, ECO:0007744|PDB:6A91, ECO:0007744|PDB:6A95
ChainResidueDetails
AASN308
AASN312
AASN330
AASN1015
AASN1034

site_idSWS_FT_FI29
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN683

site_idSWS_FT_FI30
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; atypical => ECO:0000269|PubMed:28183995, ECO:0007744|PDB:5X0M
ChainResidueDetails
AASN1028

site_idSWS_FT_FI31
Number of Residues17
DetailsTRANSMEM: Helical; Name=S1 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
APHE1172-VAL1189

site_idSWS_FT_FI32
Number of Residues22
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
AGLU1190-GLU1200
ALEU1250-THR1262

site_idSWS_FT_FI33
Number of Residues18
DetailsTRANSMEM: Helical; Name=S2 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AVAL1201-LEU1219

site_idSWS_FT_FI34
Number of Residues11
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
ALYS1220-VAL1231

site_idSWS_FT_FI35
Number of Residues17
DetailsTRANSMEM: Helical; Name=S3 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AGLY1232-PHE1249

site_idSWS_FT_FI36
Number of Residues16
DetailsTRANSMEM: Helical; Name=S4 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ALEU1263-VAL1279

219869

PDB entries from 2024-05-15

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