Human thioredoxin (oxidized form). Determined by X-ray diffraction at 2.1 Å resolution. Released 1 Aug 1996.
Explore 1ERU in 3D Show helices and sheets RCSB PDB PDBe
1ERU contains 5 α-helices and 5 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 | 2-5 | 4 | 1 |
| α-helix | 8-17 | 10 | |
| β-strand | 22-28 | 7 | 1 |
| α-helix | 33-37 | 5 | |
| α-helix | 39-48 | 10 | |
| β-strand | 52-58 | 7 | 1 |
| α-helix | 63-68 | 6 | |
| β-strand | 76-81 | 6 | 1 |
| β-strand | 84-90 | 7 | 1 |
| α-helix | 94-104 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Thioredoxin | A | protein | 105 | Homo sapiens | P10599 (AlphaFold model) |
>1ERU_1 THIOREDOXIN (chains A) MVKQIESKTAFQEALDAAGDKLVVVDFSATWCGPCKMIKPFFHSLSEKYSNVIFLEVDVD DCQDVASECEVKCMPTFQFFKKGQKVGEFSGANKEKLEATINELV
Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer. Weichsel, A., Gasdaska, J.R., Powis, G. et al. Structure (1996) 4:735-751. DOI 10.1016/S0969-2126(96)00079-2 · PubMed
Other PDB entries of the same protein (UniProt P10599 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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