MolNFT v1 · #166500 · protein
Extended sensor paddles with bound lipids revealed in mechanosensitive channel ynai
6URT: “Extended sensor paddles with bound lipids revealed in mechanosensitive channel ynai”. Electron microscopy, 1 ligand (QGD). MolNFT v1 #166500 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6URT
- Type
- protein
- Length
- 2,317 residues
- Chains
- 7
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0AEB5
- Ligands
- QGD
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| G, A, B, C, D, E, F | — | protein | 331 | — | P0AEB5 |
Ligands and binding sites
- QGD · O-{(R)-hydroxy[(2r)-3-(icosyloxy)-2-(tetradecanoyloxy) propoxy]phosphoryl}-L-serine · ligand · 7 copies · chains G, F, A, B, C, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6URT · Extended Sensor Paddles with Bound Lipids Revealed in Mechanosensitive Channel YnaI · the same entry in another collection · chain F against F, TM-score 1.00
- P0AEB5 · AlphaFold monomer V2.0 prediction for low conductance mechanosensitive channel ynai… · a predicted model of the same protein · chain G against A, TM-score 0.84
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 P0AEB5
- Elsewhere: RCSB PDB 6URT · PDBe 6URT · UniProt P0AEB5
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