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
- 5NUQ
- Type
- protein
- Length
- 2,439 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P02931, A0A0U8E5M0
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | — | protein | 340 | — | P02931 |
| G | — | protein | 200 | — | A0A0U8E5M0 |
| H | — | protein | 199 | — | A0A0U8E5M0 |
Ligands and binding sites
- C8E · (hydroxyethyloxy)tri(ethyloxy)octane · additive · 9 copies · chains A, B, D, F, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5NUQ · Structural basis for maintenance of bacterial outer membrane lipid asymmetry · the same entry in another collection · chain H against H, TM-score 1.00
- P02931 · AlphaFold monomer V2.0 prediction for outer membrane porin F (P02931) · a predicted model of the same protein · 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 P02931
- Every structure of UniProt A0A0U8E5M0
- Elsewhere: RCSB PDB 5NUQ · PDBe 5NUQ · UniProt P02931 · UniProt A0A0U8E5M0
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