Crystal structure of beta-2-microglobulin D76S mutant. Determined by X-ray diffraction at 1.15 Å resolution. Released 3 Aug 2022.
Explore 7NMR in 3D Show helices and sheets RCSB PDB PDBe
7NMR contains 2 α-helices and 10 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 | 3 | 1 | 1 |
| α-helix | 4-5 | 2 | |
| β-strand | 6-12 | 7 | 2 |
| β-strand | 22-30 | 9 | 2 |
| β-strand | 31 | 1 | 1 |
| β-strand | 36-41 | 6 | 3 |
| β-strand | 44-45 | 2 | 3 |
| α-helix | 46 | 1 | |
| β-strand | 51-56 | 6 | 2 |
| β-strand | 62-69 | 8 | 2 |
| β-strand | 78-83 | 6 | 3 |
| β-strand | 91-94 | 4 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Beta-2-microglobulin | AAA | protein | 98 | Homo sapiens | P61769 (AlphaFold model) |
>7NMR_1 Beta-2-microglobulin (chains AAA) MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKD WSFYLLYYTEFTPTEKSEYACRVNHVTLSQPKIVKWDR
The effect of mutation on an aggregation-prone protein: An in vivo, in vitro, and in silico analysis. Guthertz, N., van der Kant, R., Martinez, R.M. et al. Proc Natl Acad Sci U S A (2022) 119:e2200468119-e2200468119. DOI 10.1073/pnas.2200468119 · PubMed
Other PDB entries of the same protein (UniProt P61769 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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