HsUbc2b. Determined by solution NMR. Released 9 Sept 2003.
Explore 1JAS in 3D Show helices and sheets RCSB PDB PDBe
1JAS contains 7 α-helices and 7 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 | 4-18 | 15 | |
| β-strand | 24-28 | 5 | 1 |
| β-strand | 35-41 | 7 | 1 |
| α-helix | 42-43 | 2 | |
| β-strand | 52-58 | 7 | 1 |
| β-strand | 69-72 | 4 | 1 |
| β-strand | 81 | 1 | 2 |
| β-strand | 86 | 1 | 1 |
| β-strand | 87 | 1 | 2 |
| α-helix | 90-92 | 3 | |
| α-helix | 102-114 | 13 | |
| α-helix | 124-131 | 8 | |
| α-helix | 134-146 | 13 | |
| α-helix | 147-150 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin-conjugating enzyme E2-17 kda | A | protein | 152 | Homo sapiens | P63146 (AlphaFold model) |
>1JAS_1 UBIQUITIN-CONJUGATING ENZYME E2-17 KDA (chains A) MSTPARRRLMRDFKRLQEDPPVGVSGAPSENNIMQWNAVIFGPEGTPFEDGTFKLVIEFS EEYPNKPPTVRFLSKMFHPNVYADGSICLDILQNRWSPTYDVSSILTSIQSLLDEPNPNS PANSQAAQLYQENKREYEKRVSAIVEQSWNDS
The NMR structure of the class I human ubiquitin-conjugating enzyme 2b. Miura, T., Klaus, W., Ross, A. et al. J Biomol NMR (2002) 22:89-92. DOI 10.1023/A:1013807519703 · PubMed
Other PDB entries of the same protein (UniProt P63146 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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