Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

9DK5

Cryo-EM structure of human Nav1.6 in complex with PaurTx3

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001508	biological_process	action potential
A	0001518	cellular_component	voltage-gated sodium channel complex
A	0002102	cellular_component	podosome
A	0005248	molecular_function	voltage-gated sodium channel activity
A	0005272	molecular_function	sodium channel activity
A	0005515	molecular_function	protein binding
A	0005886	cellular_component	plasma membrane
A	0006811	biological_process	monoatomic ion transport
A	0006814	biological_process	sodium ion transport
A	0007422	biological_process	peripheral nervous system development
A	0016020	cellular_component	membrane
A	0030018	cellular_component	Z disc
A	0030424	cellular_component	axon
A	0031402	molecular_function	sodium ion binding
A	0031410	cellular_component	cytoplasmic vesicle
A	0033268	cellular_component	node of Ranvier
A	0034220	biological_process	monoatomic ion transmembrane transport
A	0034702	cellular_component	monoatomic ion channel complex
A	0035725	biological_process	sodium ion transmembrane transport
A	0042552	biological_process	myelination
A	0043194	cellular_component	axon initial segment
A	0086002	biological_process	cardiac muscle cell action potential involved in contraction
A	0086010	biological_process	membrane depolarization during action potential
H	0005576	cellular_component	extracellular region
H	0005615	cellular_component	extracellular space
H	0017080	molecular_function	sodium channel regulator activity
H	0019871	molecular_function	sodium channel inhibitor activity
H	0044493	biological_process	venom-mediated inhibition of voltage-gated sodium channel activity
H	0090729	molecular_function	toxin activity
H	0099106	molecular_function	ion channel regulator activity
I	0005576	cellular_component	extracellular region
I	0005615	cellular_component	extracellular space
I	0017080	molecular_function	sodium channel regulator activity
I	0019871	molecular_function	sodium channel inhibitor activity
I	0044493	biological_process	venom-mediated inhibition of voltage-gated sodium channel activity
I	0090729	molecular_function	toxin activity
I	0099106	molecular_function	ion channel regulator activity
J	0005576	cellular_component	extracellular region
J	0005615	cellular_component	extracellular space
J	0017080	molecular_function	sodium channel regulator activity
J	0019871	molecular_function	sodium channel inhibitor activity
J	0044493	biological_process	venom-mediated inhibition of voltage-gated sodium channel activity
J	0090729	molecular_function	toxin activity
J	0099106	molecular_function	ion 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
A	TYR1234-THR1252

site_id	PS60021
Number of Residues	29
Details	HWTX_1 Huwentoxin-1 family signature. CLgFlwkCnpsndkCCrpnlv.CsrkdKWC

Chain	Residue	Details
H	CYS2-CYS30

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	18
Details	Transmembrane: {"description":"Helical; Name=S1 of repeat I","evidences":[{"source":"UniProtKB","id":"D0E0C2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	307
Details	Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=S2 of repeat I","evidences":[{"source":"UniProtKB","id":"D0E0C2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	179
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	17
Details	Transmembrane: {"description":"Helical; Name=S3 of repeat I","evidences":[{"source":"UniProtKB","id":"D0E0C2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	16
Details	Transmembrane: {"description":"Helical; Name=S4 of repeat I","evidences":[{"source":"UniProtKB","id":"D0E0C2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	19
Details	Transmembrane: {"description":"Helical; Name=S5 of repeat I","evidences":[{"source":"UniProtKB","id":"D0E0C2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	87
Details	Intramembrane: {"description":"Pore-forming","evidences":[{"source":"UniProtKB","id":"D0E0C2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=S6 of repeat I","evidences":[{"source":"UniProtKB","id":"D0E0C2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	18
Details	Transmembrane: {"description":"Helical; Name=S1 of repeat II","evidences":[{"source":"UniProtKB","id":"D0E0C2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	19
Details	Transmembrane: {"description":"Helical; Name=S2 of repeat II","evidences":[{"source":"UniProtKB","id":"D0E0C2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	19
Details	Transmembrane: {"description":"Helical; Name=S3 of repeat II","evidences":[{"source":"UniProtKB","id":"D0E0C2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	17
Details	Transmembrane: {"description":"Helical; Name=S4 of repeat II","evidences":[{"source":"UniProtKB","id":"D0E0C2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	18
Details	Transmembrane: {"description":"Helical; Name=S5 of repeat II","evidences":[{"source":"UniProtKB","id":"D0E0C2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=S6 of repeat II","evidences":[{"source":"UniProtKB","id":"D0E0C2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	17
Details	Transmembrane: {"description":"Helical; Name=S1 of repeat III","evidences":[{"source":"UniProtKB","id":"D0E0C2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	18
Details	Transmembrane: {"description":"Helical; Name=S2 of repeat III","evidences":[{"source":"UniProtKB","id":"D0E0C2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	18
Details	Transmembrane: {"description":"Helical; Name=S3 of repeat III","evidences":[{"source":"UniProtKB","id":"D0E0C2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	18
Details	Transmembrane: {"description":"Helical; Name=S4 of repeat III","evidences":[{"source":"UniProtKB","id":"D0E0C2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	19
Details	Transmembrane: {"description":"Helical; Name=S5 of repeat III","evidences":[{"source":"UniProtKB","id":"D0E0C2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	21
Details	Transmembrane: {"description":"Helical; Name=S6 of repeat III","evidences":[{"source":"UniProtKB","id":"D0E0C2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	17
Details	Transmembrane: {"description":"Helical; Name=S1 of repeat IV","evidences":[{"source":"UniProtKB","id":"D0E0C2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	18
Details	Transmembrane: {"description":"Helical; Name=S2 of repeat IV","evidences":[{"source":"UniProtKB","id":"D0E0C2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	17
Details	Transmembrane: {"description":"Helical; Name=S3 of repeat IV","evidences":[{"source":"UniProtKB","id":"D0E0C2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	16
Details	Transmembrane: {"description":"Helical; Name=S4 of repeat IV","evidences":[{"source":"UniProtKB","id":"D0E0C2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI26
Number of Residues	17
Details	Transmembrane: {"description":"Helical; Name=S5 of repeat IV","evidences":[{"source":"UniProtKB","id":"D0E0C2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI27
Number of Residues	22
Details	Transmembrane: {"description":"Helical; Name=S6 of repeat IV","evidences":[{"source":"UniProtKB","id":"D0E0C2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI28
Number of Residues	315
Details	Repeat: {"description":"III","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI29
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"36823201","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8GZ1","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI30
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by PKC","evidences":[{"source":"UniProtKB","id":"Q15858","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI31
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI32
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"36823201","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8GZ1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8GZ2","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI33
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"36696443","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36823201","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8FHD","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"8GZ1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8GZ2","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI34
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (high mannose) asparagine","evidences":[{"source":"PubMed","id":"36696443","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36823201","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8FHD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8GZ1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8GZ2","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI35
Number of Residues	21
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"30190309","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6AGF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI36
Number of Residues	128
Details	Domain: {"description":"Ig-like C2-type"}

Chain

Residue

Details

site_id	SWS_FT_FI37
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"30765606","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36696443","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6J8G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J8H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J8I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J8J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8FHD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI38
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"30190309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30765606","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36696443","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6AGF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J8G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J8H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J8I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J8J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8FHD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI39
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"30765606","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36696443","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36823201","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6J8G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J8H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J8I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J8J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8FHD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8GZ1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8GZ2","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI40
Number of Residues	99
Details	Peptide: {"description":"Beta-theraphotoxin-Ps1a","featureId":"PRO_0000045003","evidences":[{"source":"PubMed","id":"16267209","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)