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7XMF

Cryo-EM structure of human NaV1.7/beta1/beta2-Nav1.7-IN2

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
A0006091biological_processgeneration of precursor metabolites and energy
A0006811biological_processmonoatomic ion transport
A0006814biological_processsodium ion transport
A0006954biological_processinflammatory response
A0007623biological_processcircadian rhythm
A0008218biological_processbioluminescence
A0009636biological_processresponse to toxic substance
A0009791biological_processpost-embryonic development
A0016020cellular_componentmembrane
A0019233biological_processsensory perception of pain
A0030424cellular_componentaxon
A0034220biological_processmonoatomic ion transmembrane transport
A0034702cellular_componentmonoatomic ion channel complex
A0035725biological_processsodium ion transmembrane transport
A0042995cellular_componentcell projection
A0043005cellular_componentneuron projection
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
B0001518cellular_componentvoltage-gated sodium channel complex
B0006091biological_processgeneration of precursor metabolites and energy
B0006814biological_processsodium ion transport
B0008218biological_processbioluminescence
B0017080molecular_functionsodium channel regulator activity
C0016020cellular_componentmembrane
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues129
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
CMET30-ALA159
ALYS1465-LEU1527
AVAL1576-ILE1587
AALA1636-VAL1654
AARG174-PRO187
APRO229-ASP247
AVAL400-VAL755
AVAL806-SER819
AGLY860-ILE875
AILE979-LEU1204
ATHR1255-VAL1268
AILE1315-PHE1331

site_idSWS_FT_FI2
Number of Residues20
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
CVAL160-VAL180

site_idSWS_FT_FI3
Number of Residues34
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
CLYS181-LYS215
ASER1288-LEU1295
AASN1352-ALA1403
ALYS1426-ILE1442
AVAL1546-ILE1556
APRO1606-GLY1618
AASP1673-ILE1694
ALYS1718-SER1747
AASN206-SER211
AMET268-THR346
AARG372-TYR378
AVAL775-GLY785
ALEU840-ARG841
ACYS895-VAL923
ALEU945-LEU957
ALYS1223-TYR1235

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Binds SCN2A => ECO:0000305|PubMed:30765605
ChainResidueDetails
CTYR56
CARG135

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P54900
ChainResidueDetails
CSER192
BASN114

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P54900
ChainResidueDetails
CTHR204

site_idSWS_FT_FI7
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
CASN42
CASN74

site_idSWS_FT_FI8
Number of Residues1
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
CASN66
ALEU924-CYS944
ATHR1404-PRO1425
ATHR1695-PRO1717

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
ALEU756-ASN774

site_idSWS_FT_FI11
Number of Residues19
DetailsTRANSMEM: Helical; Name=S2 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AILE786-GLN805

site_idSWS_FT_FI12
Number of Residues19
DetailsTRANSMEM: Helical; Name=S3 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ALEU820-LEU839

site_idSWS_FT_FI13
Number of Residues17
DetailsTRANSMEM: Helical; Name=S4 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AVAL842-ILE859

site_idSWS_FT_FI14
Number of Residues18
DetailsTRANSMEM: Helical; Name=S5 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AILE876-GLU894

site_idSWS_FT_FI15
Number of Residues20
DetailsTRANSMEM: Helical; Name=S6 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AVAL958-ALA978

site_idSWS_FT_FI16
Number of Residues17
DetailsTRANSMEM: Helical; Name=S1 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ASER1205-ILE1222

site_idSWS_FT_FI17
Number of Residues18
DetailsTRANSMEM: Helical; Name=S2 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AILE1236-PHE1254

site_idSWS_FT_FI18
Number of Residues18
DetailsTRANSMEM: Helical; Name=S3 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ASER1269-LYS1287

site_idSWS_FT_FI19
Number of Residues18
DetailsTRANSMEM: Helical; Name=S4 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AARG1296-LEU1314

site_idSWS_FT_FI20
Number of Residues19
DetailsTRANSMEM: Helical; Name=S5 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ATRP1332-ILE1351

site_idSWS_FT_FI21
Number of Residues21
DetailsTRANSMEM: Helical; Name=S6 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
APHE1443-LYS1464

site_idSWS_FT_FI22
Number of Residues17
DetailsTRANSMEM: Helical; Name=S1 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AASN1528-GLU1545

site_idSWS_FT_FI23
Number of Residues18
DetailsTRANSMEM: Helical; Name=S2 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ALEU1557-THR1575

site_idSWS_FT_FI24
Number of Residues17
DetailsTRANSMEM: Helical; Name=S3 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AILE1588-SER1605

site_idSWS_FT_FI25
Number of Residues16
DetailsTRANSMEM: Helical; Name=S4 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AARG1619-PHE1635

site_idSWS_FT_FI26
Number of Residues17
DetailsTRANSMEM: Helical; Name=S5 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AMET1655-GLU1672

site_idSWS_FT_FI27
Number of Residues22
DetailsTRANSMEM: Helical; Name=S6 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
APHE1748-SER1770

site_idSWS_FT_FI28
Number of Residues2
DetailsSITE: Is directly targeted by the spider protoxin-II => ECO:0000269|PubMed:30661758
ChainResidueDetails
AVAL833
AARG838

site_idSWS_FT_FI29
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:25240195
ChainResidueDetails
AGLY1501

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
AGLN1363
ASER1377
ALYS1386

221371

PDB entries from 2024-06-19

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