Research workbench
Voltage-gated sodium channel NAV1.4 iq domain in complex with CA2+/CALMODULIN
Analyse Voltage-gated sodium channel NAV1.4 iq domain in complex with CA2+/CALMODULIN in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MUE
- Type
- protein
- Length
- 154 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0DP23, P15390
- Ligands
- CA
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 139 | — | P0DP23 |
| B | — | protein | 15 | — | P15390 |
Ligands and binding sites
- CA · Calcium ion · metal · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6MUE · Voltage-gated sodium channel NaV1.4 IQ domain in complex with Ca2+/Calmodulin · the same entry in another collection · chain A against A, TM-score 1.00
- P0DP23 · AlphaFold monomer V2.0 prediction for calmodulin-1 (P0DP23) · a predicted model of the same protein · chain A against A, TM-score 0.63
- P15390 · AlphaFold monomer V2.0 prediction for sodium channel protein type 4 subunit alpha (P15390) · a predicted model of the same protein · chain B against A, TM-score 0.61
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P0DP23
- Every structure of UniProt P15390
- Elsewhere: RCSB PDB 6MUE · PDBe 6MUE · UniProt P0DP23 · UniProt P15390
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