Solution Structure of the Ubiquitin-like Domain in Human FAS-associated factor 1 (hFAF1). Determined by solution NMR. Released 9 Oct 2007.
Explore 2DZM in 3D Show helices and sheets RCSB PDB PDBe
2DZM contains 2 α-helices and 6 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 | 9-15 | 7 | 1 |
| β-strand | 20-26 | 7 | 1 |
| β-strand | 30 | 1 | 2 |
| α-helix | 31-42 | 12 | |
| β-strand | 51-52 | 2 | 1 |
| β-strand | 64 | 1 | 2 |
| α-helix | 65-68 | 4 | |
| β-strand | 73-78 | 6 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| FAS-associated factor 1 | A | protein | 100 | Homo sapiens | Q9UNN5 (AlphaFold model) |
>2DZM_1 FAS-associated factor 1 (chains A) GSSGSSGRMLDFRVEYRDRNVDVVLEDTCTVGEIKQILENELQIPVSKMLLKGWKTGDVE DSTVLKSLHLPKNNSLYVLTPDLPPPSSSSHAGALQESLN
Solution Structure of the Ubiquitin-like Domain in Human FAS-associated factor 1 (hFAF1). Zhao, C., Sato, M., Koshiba, S. et al. To be published.
Other PDB entries of the same protein (UniProt Q9UNN5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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