Research workbench
F233W mutant of the KV2.1 paddle-KV1.2 chimera channel
Analyse F233W mutant of the KV2.1 paddle-KV1.2 chimera channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LNM
- Type
- protein
- Length
- 1,359 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P62483, P63142, P15387
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 326 | — | P62483 |
| B | — | protein | 389 | — | P63142, P15387 |
| D | — | protein | 318 | — | P63142, P15387 |
Compared structures
- 3LNM · F233W mutant of the Kv2.1 paddle-Kv1.2 chimera channel · the same entry in another collection · chain A against A, TM-score 1.00
- P62483 · AlphaFold monomer V2.0 prediction for voltage-gated potassium channel subunit beta-2… · a predicted model of the same protein · chain A against A, TM-score 0.99
- P63142 · AlphaFold monomer V2.0 prediction for potassium voltage-gated channel subfamily a member… · a predicted model of the same protein · chain B against A, TM-score 0.96
- P15387 · AlphaFold monomer V2.0 prediction for potassium voltage-gated channel subfamily B member… · a predicted model of the same protein · chain B against A, TM-score 0.73
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 P62483
- Every structure of UniProt P63142
- Every structure of UniProt P15387
- Elsewhere: RCSB PDB 3LNM · PDBe 3LNM · UniProt P62483 · UniProt P63142 · UniProt P15387
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