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

8GZ1

Cryo-EM structure of human NaV1.6/beta1/beta2,apo state

Functional Information from GO Data
ChainGOidnamespacecontents
B0001508biological_processaction potential
B0001518cellular_componentvoltage-gated sodium channel complex
B0002102cellular_componentpodosome
B0005216molecular_functionmonoatomic ion channel activity
B0005248molecular_functionvoltage-gated sodium channel activity
B0005261molecular_functionmonoatomic cation channel activity
B0005272molecular_functionsodium channel activity
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0006814biological_processsodium ion transport
B0007422biological_processperipheral nervous system development
B0016020cellular_componentmembrane
B0019228biological_processneuronal action potential
B0021554biological_processoptic nerve development
B0030018cellular_componentZ disc
B0030054cellular_componentcell junction
B0030424cellular_componentaxon
B0031402molecular_functionsodium ion binding
B0031410cellular_componentcytoplasmic vesicle
B0033268cellular_componentnode of Ranvier
B0034220biological_processmonoatomic ion transmembrane transport
B0034702cellular_componentmonoatomic ion channel complex
B0035725biological_processsodium ion transmembrane transport
B0042552biological_processmyelination
B0042995cellular_componentcell projection
B0043194cellular_componentaxon initial segment
B0048787cellular_componentpresynaptic active zone membrane
B0055085biological_processtransmembrane transport
B0070161cellular_componentanchoring junction
B0086002biological_processcardiac muscle cell action potential involved in contraction
B0098688cellular_componentparallel fiber to Purkinje cell synapse
B0098839cellular_componentpostsynaptic density membrane
B0098978cellular_componentglutamatergic synapse
C0016020cellular_componentmembrane
D0001518cellular_componentvoltage-gated sodium channel complex
D0006814biological_processsodium ion transport
D0017080molecular_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
BTYR1234-THR1252

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues127
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:36823201, ECO:0007744|PDB:8GZ2
ChainResidueDetails
CMET30-THR157
BGLY1461-ALA1523
BLYS1572-ILE1583
BLYS1632-ALA1650
BLEU1766-CYS1980
BARG180-PRO193
BPRO235-ASP253
BVAL409-PRO753
BLEU804-TRP817
BTRP858-GLY873
BLEU977-TRP1199
BLYS1250-ALA1263
BPHE1310-SER1326

site_idSWS_FT_FI2
Number of Residues21
DetailsTRANSMEM: Helical => ECO:0000305|PubMed:36823201, ECO:0007744|PDB:8GZ2
ChainResidueDetails
CVAL158-VAL179

site_idSWS_FT_FI3
Number of Residues35
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:36823201, ECO:0007744|PDB:8GZ2
ChainResidueDetails
CVAL180-LYS215
BALA1283-GLY1290
BASN1347-VAL1399
BALA1422-ILE1438
BGLU1542-ASN1552
BLEU1602-THR1614
BGLY1669-THR1690
BILE1714-GLY1742
BASN212-SER217
BMET274-THR355
BARG381-TYR387
BGLU773-HIS783
BGLU838-GLY839
BGLY893-ASP921
BASP943-ILE955
BGLU1218-THR1230

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
DASN114

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
BPHE922-TRP942
BGLY1400-ALA1421
BPHE1691-PRO1713

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=S6 of repeat I => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
BMET388-ALA408

site_idSWS_FT_FI10
Number of Residues18
DetailsTRANSMEM: Helical; Name=S1 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
BPHE754-MET772

site_idSWS_FT_FI11
Number of Residues19
DetailsTRANSMEM: Helical; Name=S2 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
BVAL784-LYS803

site_idSWS_FT_FI12
Number of Residues19
DetailsTRANSMEM: Helical; Name=S3 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
BASN818-VAL837

site_idSWS_FT_FI13
Number of Residues17
DetailsTRANSMEM: Helical; Name=S4 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
BLEU840-SER857

site_idSWS_FT_FI14
Number of Residues18
DetailsTRANSMEM: Helical; Name=S5 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
BALA874-VAL892

site_idSWS_FT_FI15
Number of Residues20
DetailsTRANSMEM: Helical; Name=S6 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
BVAL956-LEU976

site_idSWS_FT_FI16
Number of Residues17
DetailsTRANSMEM: Helical; Name=S1 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
BPHE1200-PHE1217

site_idSWS_FT_FI17
Number of Residues18
DetailsTRANSMEM: Helical; Name=S2 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
BILE1231-LEU1249

site_idSWS_FT_FI18
Number of Residues18
DetailsTRANSMEM: Helical; Name=S3 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
BTRP1264-ASN1282

site_idSWS_FT_FI19
Number of Residues18
DetailsTRANSMEM: Helical; Name=S4 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
BALA1291-ARG1309

site_idSWS_FT_FI20
Number of Residues19
DetailsTRANSMEM: Helical; Name=S5 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
BILE1327-VAL1346

site_idSWS_FT_FI21
Number of Residues21
DetailsTRANSMEM: Helical; Name=S6 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
BTYR1439-ILE1460

site_idSWS_FT_FI22
Number of Residues17
DetailsTRANSMEM: Helical; Name=S1 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
BPHE1524-VAL1541

site_idSWS_FT_FI23
Number of Residues18
DetailsTRANSMEM: Helical; Name=S2 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
BILE1553-LEU1571

site_idSWS_FT_FI24
Number of Residues17
DetailsTRANSMEM: Helical; Name=S3 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
BGLY1584-PHE1601

site_idSWS_FT_FI25
Number of Residues16
DetailsTRANSMEM: Helical; Name=S4 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
BLEU1615-ILE1631

site_idSWS_FT_FI26
Number of Residues17
DetailsTRANSMEM: Helical; Name=S5 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
BLEU1651-PHE1668

site_idSWS_FT_FI27
Number of Residues22
DetailsTRANSMEM: Helical; Name=S6 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
BILE1743-ILE1765

site_idSWS_FT_FI28
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:36823201, ECO:0007744|PDB:8GZ1
ChainResidueDetails
BGLU373
BGLU936
BGLU939

site_idSWS_FT_FI29
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O88420
ChainResidueDetails
BSER518
BSER520

site_idSWS_FT_FI30
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000250|UniProtKB:Q15858
ChainResidueDetails
BSER1497

site_idSWS_FT_FI31
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN215
BASN1383

site_idSWS_FT_FI32
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:36823201, ECO:0007744|PDB:8GZ1, ECO:0007744|PDB:8GZ2
ChainResidueDetails
BASN289

site_idSWS_FT_FI33
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
BASN295
BASN308
BASN1358
BASN1372

site_idSWS_FT_FI34
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
BASN326

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon