MolNFT v1 · #98840 · protein
Structure of the eag domain-cnbhd complex of the mouse EAG1 channel
4LLO: “Structure of the eag domain-cnbhd complex of the mouse EAG1 channel”. X-ray diffraction. MolNFT v1 #98840 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4LLO
- Type
- protein
- Length
- 1,143 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q60603
Structure
x-ray diffraction · 7 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 173 | — | Q60603 |
| B, F | — | protein | 121 | — | Q60603 |
| C | — | protein | 168 | — | Q60603 |
| D | — | protein | 110 | — | Q60603 |
| E | — | protein | 171 | — | Q60603 |
| G | — | protein | 169 | — | Q60603 |
| H | — | protein | 110 | — | Q60603 |
Compared structures
- 4LLO · Structure of the eag domain-CNBHD complex of the mouse EAG1 channel · the same entry in another collection · chain H against H, TM-score 1.00
- Q60603 · AlphaFold monomer V2.0 prediction for potassium voltage-gated channel subfamily H member… · a predicted model of the same protein · chain H against A, TM-score 0.99
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 Q60603
- Elsewhere: RCSB PDB 4LLO · PDBe 4LLO · UniProt Q60603
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