8GZ1
Cryo-EM structure of human NaV1.6/beta1/beta2,apo state
Functional Information from GO Data
Chain | GOid | namespace | contents |
B | 0001508 | biological_process | action potential |
B | 0001518 | cellular_component | voltage-gated sodium channel complex |
B | 0002102 | cellular_component | podosome |
B | 0005216 | molecular_function | monoatomic ion channel activity |
B | 0005248 | molecular_function | voltage-gated sodium channel activity |
B | 0005261 | molecular_function | monoatomic cation channel activity |
B | 0005272 | molecular_function | sodium channel activity |
B | 0005515 | molecular_function | protein binding |
B | 0005886 | cellular_component | plasma membrane |
B | 0006811 | biological_process | monoatomic ion transport |
B | 0006814 | biological_process | sodium ion transport |
B | 0007422 | biological_process | peripheral nervous system development |
B | 0016020 | cellular_component | membrane |
B | 0019228 | biological_process | neuronal action potential |
B | 0021554 | biological_process | optic nerve development |
B | 0030018 | cellular_component | Z disc |
B | 0030054 | cellular_component | cell junction |
B | 0030424 | cellular_component | axon |
B | 0031402 | molecular_function | sodium ion binding |
B | 0031410 | cellular_component | cytoplasmic vesicle |
B | 0033268 | cellular_component | node of Ranvier |
B | 0034220 | biological_process | monoatomic ion transmembrane transport |
B | 0034702 | cellular_component | monoatomic ion channel complex |
B | 0035725 | biological_process | sodium ion transmembrane transport |
B | 0042552 | biological_process | myelination |
B | 0042995 | cellular_component | cell projection |
B | 0043194 | cellular_component | axon initial segment |
B | 0048787 | cellular_component | presynaptic active zone membrane |
B | 0055085 | biological_process | transmembrane transport |
B | 0070161 | cellular_component | anchoring junction |
B | 0086002 | biological_process | cardiac muscle cell action potential involved in contraction |
B | 0098688 | cellular_component | parallel fiber to Purkinje cell synapse |
B | 0098839 | cellular_component | postsynaptic density membrane |
B | 0098978 | cellular_component | glutamatergic synapse |
C | 0016020 | cellular_component | membrane |
D | 0001518 | cellular_component | voltage-gated sodium channel complex |
D | 0006814 | biological_process | sodium ion transport |
D | 0017080 | molecular_function | sodium channel regulator activity |
Functional Information from PROSITE/UniProt
site_id | PS00878 |
Number of Residues | 19 |
Details | ODR_DC_2_1 Orn/DAP/Arg decarboxylases family 2 pyridoxal-P attachment site. YAdKVFtyifILemLlkwT |
Chain | Residue | Details |
B | TYR1234-THR1252 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 129 |
Details | TOPO_DOM: Extracellular => ECO:0000255 |
Chain | Residue | Details |
C | MET30-ALA159 | |
B | GLY1461-ALA1523 | |
B | LYS1572-ILE1583 | |
B | LYS1632-ALA1650 | |
B | LEU1766-CYS1980 | |
B | ARG180-PRO193 | |
B | PRO235-ASP253 | |
B | VAL409-PRO753 | |
B | LEU804-TRP817 | |
B | TRP858-GLY873 | |
B | LEU977-TRP1199 | |
B | LYS1250-ALA1263 | |
B | PHE1310-SER1326 |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
C | VAL160-VAL180 |
site_id | SWS_FT_FI3 |
Number of Residues | 34 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
C | LYS181-LYS215 | |
B | ALA1283-GLY1290 | |
B | ASN1347-VAL1399 | |
B | ALA1422-ILE1438 | |
B | GLU1542-ASN1552 | |
B | LEU1602-THR1614 | |
B | GLY1669-THR1690 | |
B | ILE1714-GLY1742 | |
B | ASN212-SER217 | |
B | MET274-THR355 | |
B | ARG381-TYR387 | |
B | GLU773-HIS783 | |
B | GLU838-GLY839 | |
B | GLY893-ASP921 | |
B | ASP943-ILE955 | |
B | GLU1218-THR1230 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Binds SCN2A => ECO:0000305|PubMed:30765605 |
Chain | Residue | Details |
C | TYR56 | |
C | ARG135 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P54900 |
Chain | Residue | Details |
C | SER192 | |
D | ASN114 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P54900 |
Chain | Residue | Details |
C | THR204 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
C | ASN42 | |
C | ASN74 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:30765606, ECO:0007744|PDB:6J8G, ECO:0007744|PDB:6J8H, ECO:0007744|PDB:6J8I, ECO:0007744|PDB:6J8J |
Chain | Residue | Details |
C | ASN66 | |
B | PHE922-TRP942 | |
B | GLY1400-ALA1421 | |
B | PHE1691-PRO1713 |
site_id | SWS_FT_FI9 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S6 of repeat I => ECO:0000250|UniProtKB:D0E0C2 |
Chain | Residue | Details |
B | MET388-ALA408 |
site_id | SWS_FT_FI10 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S1 of repeat II => ECO:0000250|UniProtKB:D0E0C2 |
Chain | Residue | Details |
B | PHE754-MET772 |
site_id | SWS_FT_FI11 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=S2 of repeat II => ECO:0000250|UniProtKB:D0E0C2 |
Chain | Residue | Details |
B | VAL784-LYS803 |
site_id | SWS_FT_FI12 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=S3 of repeat II => ECO:0000250|UniProtKB:D0E0C2 |
Chain | Residue | Details |
B | ASN818-VAL837 |
site_id | SWS_FT_FI13 |
Number of Residues | 17 |
Details | TRANSMEM: Helical; Name=S4 of repeat II => ECO:0000250|UniProtKB:D0E0C2 |
Chain | Residue | Details |
B | LEU840-SER857 |
site_id | SWS_FT_FI14 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S5 of repeat II => ECO:0000250|UniProtKB:D0E0C2 |
Chain | Residue | Details |
B | ALA874-VAL892 |
site_id | SWS_FT_FI15 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=S6 of repeat II => ECO:0000250|UniProtKB:D0E0C2 |
Chain | Residue | Details |
B | VAL956-LEU976 |
site_id | SWS_FT_FI16 |
Number of Residues | 17 |
Details | TRANSMEM: Helical; Name=S1 of repeat III => ECO:0000250|UniProtKB:D0E0C2 |
Chain | Residue | Details |
B | PHE1200-PHE1217 |
site_id | SWS_FT_FI17 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S2 of repeat III => ECO:0000250|UniProtKB:D0E0C2 |
Chain | Residue | Details |
B | ILE1231-LEU1249 |
site_id | SWS_FT_FI18 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S3 of repeat III => ECO:0000250|UniProtKB:D0E0C2 |
Chain | Residue | Details |
B | TRP1264-ASN1282 |
site_id | SWS_FT_FI19 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S4 of repeat III => ECO:0000250|UniProtKB:D0E0C2 |
Chain | Residue | Details |
B | ALA1291-ARG1309 |
site_id | SWS_FT_FI20 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=S5 of repeat III => ECO:0000250|UniProtKB:D0E0C2 |
Chain | Residue | Details |
B | ILE1327-VAL1346 |
site_id | SWS_FT_FI21 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=S6 of repeat III => ECO:0000250|UniProtKB:D0E0C2 |
Chain | Residue | Details |
B | TYR1439-ILE1460 |
site_id | SWS_FT_FI22 |
Number of Residues | 17 |
Details | TRANSMEM: Helical; Name=S1 of repeat IV => ECO:0000250|UniProtKB:D0E0C2 |
Chain | Residue | Details |
B | PHE1524-VAL1541 |
site_id | SWS_FT_FI23 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=S2 of repeat IV => ECO:0000250|UniProtKB:D0E0C2 |
Chain | Residue | Details |
B | ILE1553-LEU1571 |
site_id | SWS_FT_FI24 |
Number of Residues | 17 |
Details | TRANSMEM: Helical; Name=S3 of repeat IV => ECO:0000250|UniProtKB:D0E0C2 |
Chain | Residue | Details |
B | GLY1584-PHE1601 |
site_id | SWS_FT_FI25 |
Number of Residues | 16 |
Details | TRANSMEM: Helical; Name=S4 of repeat IV => ECO:0000250|UniProtKB:D0E0C2 |
Chain | Residue | Details |
B | LEU1615-ILE1631 |
site_id | SWS_FT_FI26 |
Number of Residues | 17 |
Details | TRANSMEM: Helical; Name=S5 of repeat IV => ECO:0000250|UniProtKB:D0E0C2 |
Chain | Residue | Details |
B | LEU1651-PHE1668 |
site_id | SWS_FT_FI27 |
Number of Residues | 22 |
Details | TRANSMEM: Helical; Name=S6 of repeat IV => ECO:0000250|UniProtKB:D0E0C2 |
Chain | Residue | Details |
B | ILE1743-ILE1765 |
site_id | SWS_FT_FI28 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:36823201, ECO:0007744|PDB:8GZ1 |
Chain | Residue | Details |
B | GLU373 | |
B | GLU936 | |
B | GLU939 |
site_id | SWS_FT_FI29 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O88420 |
Chain | Residue | Details |
B | SER518 | |
B | SER520 |
site_id | SWS_FT_FI30 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by PKC => ECO:0000250|UniProtKB:Q15858 |
Chain | Residue | Details |
B | SER1497 |
site_id | SWS_FT_FI31 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
B | ASN215 | |
B | ASN1383 |
site_id | SWS_FT_FI32 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:36823201, ECO:0007744|PDB:8GZ1, ECO:0007744|PDB:8GZ2 |
Chain | Residue | Details |
B | ASN289 |
site_id | SWS_FT_FI33 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:36696443, ECO:0000269|PubMed:36823201, ECO:0000312|PDB:8FHD, ECO:0007744|PDB:8GZ1, ECO:0007744|PDB:8GZ2 |
Chain | Residue | Details |
B | ASN295 | |
B | ASN308 | |
B | ASN1358 | |
B | ASN1372 |
site_id | SWS_FT_FI34 |
Number of Residues | 1 |
Details | CARBOHYD: 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 |
Chain | Residue | Details |
B | ASN326 |