Solution structure of the engineered protein Afae-dsc. Determined by solution NMR. Released 11 Jan 2005.
Explore 1RXL in 3D Show helices and sheets RCSB PDB PDBe
1RXL contains 0 α-helices and 15 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 | 4-6 | 3 | 1 |
| β-strand | 11-13 | 3 | 2 |
| β-strand | 28-30 | 3 | 3 |
| β-strand | 31-33 | 3 | 1 |
| β-strand | 39-44 | 6 | 2 |
| β-strand | 49 | 1 | 4 |
| β-strand | 54 | 1 | 4 |
| β-strand | 55-58 | 4 | 2 |
| β-strand | 64-66 | 3 | 2 |
| β-strand | 67-71 | 5 | 3 |
| β-strand | 77-79 | 3 | 2 |
| β-strand | 83-86 | 4 | 2 |
| β-strand | 94-100 | 7 | 3 |
| β-strand | 111-121 | 11 | 2 |
| β-strand | 129-141 | 13 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Afimbrial adhesin AFA-III | A | protein | 156 | Escherichia coli | Q57254 (AlphaFold model) |
>1RXL_1 Afimbrial adhesin AFA-III (chains A) HHHHHHGLVPRGSEECQVRVGDLTVAKTRGQLTDAAPIGPVTVQALGCNARQVALKADTD NFEQGKFFLISDNNRDKLYVNIRPMDNSAWTTDNGVFYKNDVGSWGGTIGIYVDGQQTNT PPGNYTLTLTGGYWAKDNKQGFTPSGTTGTTKLTVT
An atomic resolution model for assembly, architecture, and function of the Dr adhesins. Anderson, K.L., Billington, J., Pettigrew, D. et al. Mol Cell (2004) 15:647-657. DOI 10.1016/j.molcel.2004.08.003 · PubMed
Other PDB entries of the same protein (UniProt Q57254 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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