Research workbench
Structural basis for maintenance of bacterial outer membrane lipid asymmetry
Analyse Structural basis for maintenance of bacterial outer membrane lipid asymmetry in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NUP
- Type
- protein
- Length
- 1,634 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- D6QLY0, A0A0W8AQT6
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | — | protein | 344 | — | D6QLY0 |
| D, E | — | protein | 199 | — | A0A0W8AQT6 |
| F | — | protein | 204 | — | A0A0W8AQT6 |
Ligands and binding sites
- C8E · (hydroxyethyloxy)tri(ethyloxy)octane · additive · 19 copies · chains A, D, C, B, F, E
- LMT · Dodecyl-beta-D-maltoside · additive · 3 copies · chains B, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5NUP · Structural basis for maintenance of bacterial outer membrane lipid asymmetry · 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 D6QLY0
- Every structure of UniProt A0A0W8AQT6
- Elsewhere: RCSB PDB 5NUP · PDBe 5NUP · UniProt D6QLY0 · UniProt A0A0W8AQT6
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