Research workbench
Structure of navms pore and C-terminal domain crystallised in presence of channel blocking compound
Analyse Structure of navms pore and C-terminal domain crystallised in presence of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PA7
- Type
- protein
- Length
- 364 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0L5S6
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 92 | — | A0L5S6 |
| B | — | protein | 90 | — | A0L5S6 |
| C, D | — | protein | 91 | — | A0L5S6 |
Compared structures
- 4PA7 · Structure of NavMS pore and C-terminal domain crystallised in presence of channel… · the same entry in another collection · chain A against A, TM-score 1.00
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 A0L5S6
- Elsewhere: RCSB PDB 4PA7 · PDBe 4PA7 · UniProt A0L5S6
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