NMR structure determination of the periplasmic domain of ExbD from E.coli. Determined by solution NMR. Released 23 Oct 2007.
Explore 2PFU in 3D Show helices and sheets RCSB PDB PDBe
2PFU contains 2 α-helices and 5 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 65-69 | 5 | 1 |
| β-strand | 73-76 | 4 | 1 |
| β-strand | 79-81 | 3 | 1 |
| α-helix | 86-93 | 8 | |
| β-strand | 102-106 | 5 | 1 |
| α-helix | 112-124 | 13 | |
| β-strand | 130-131 | 2 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Biopolymer transport exbD protein | A | protein | 99 | Escherichia coli | P0ABV2 (AlphaFold model) |
>2PFU_1 Biopolymer transport exbD protein (chains A) MDVKVNLPASTSTPQPRPEKPVYLSVKADNSMFIGNDPVTDETMITALNALTEGKKDTTI FFRADKTVDYETLMKVMDTLHQAGYLKIGLVGEETAKAK
The solution structure of the periplasmic domain of the TonB system ExbD protein reveals an unexpected structural homology with siderophore-binding proteins. Garcia-Herrero, A., Peacock, R.S., Howard, S.P. et al. Mol Microbiol (2007) 66:872-889. DOI 10.1111/j.1365-2958.2007.05957.x · PubMed
Other PDB entries of the same protein (UniProt P0ABV2 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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