Solution Structure of the UBA Domain of Human NBR1. Determined by solution NMR. Released 9 Apr 2014.
Explore 2MGW in 3D Show helices and sheets RCSB PDB PDBe
2MGW contains 3 α-helices and 0 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 |
|---|---|---|---|
| α-helix | 915-925 | 11 | |
| α-helix | 932-942 | 11 | |
| α-helix | 946-956 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Next to BRCA1 gene 1 protein | A | protein | 52 | Homo sapiens | Q14596 (AlphaFold model) |
>2MGW_1 Next to BRCA1 gene 1 protein (chains A) GPLGSSEDQTAALMAHLFEMGFCDRQLNLRLLKKHNYNILQVVTELLQLNNN
Solution structure of the ubiquitin-associated (UBA) domain of human autophagy receptor NBR1 and its interaction with ubiquitin and polyubiquitin. Walinda, E., Morimoto, D., Sugase, K. et al. J Biol Chem (2014) 289:13890-13902. DOI 10.1074/jbc.M114.555441 · PubMed
Other PDB entries of the same protein (UniProt Q14596 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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