Research workbench
Solution structure of full-length apo mammalian calmodulin bound to the iq motif of the human voltage-gated sodium channel NAV1.2
Analyse Solution structure of full-length apo mammalian calmodulin bound to the iq… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BUT
- Type
- protein
- Length
- 179 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calmodulin-1; Sodium channel protein type 2 subunit alpha
- UniProt
- P0DP23, Q99250
- Pockets
- 1 · best druggability 0.52
Structure
solution nmr · 2 distinct chains · 59% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calmodulin-1 | protein | 148 | 57% helix, 7% strand | P0DP23 |
| B | Sodium channel protein type 2 subunit alpha | protein | 31 | 71% helix, 0% strand | Q99250 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 203 | 0.52 | 0.77 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1127 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 6BUT · Solution structure of full-length apo mammalian calmodulin bound to the IQ motif of the… · the same entry in another collection · chain A against A, TM-score 1.00
- Q99250 · AlphaFold monomer V2.0 prediction for sodium channel protein type 2 subunit alpha (Q99250) · a predicted model of the same protein · chain B against A, TM-score 0.62
- P0DP23 · AlphaFold monomer V2.0 prediction for calmodulin-1 (P0DP23) · a predicted model of the same protein · chain A against A, TM-score 0.49
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 Q99250
- Elsewhere: RCSB PDB 6BUT · PDBe 6BUT · UniProt P0DP23 · UniProt Q99250
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