Human thioredoxin (oxidized with diamide). Determined by X-ray diffraction at 2.1 Å resolution. Released 25 Feb 1998.
Explore 1AUC in 3D Show helices and sheets RCSB PDB PDBe
1AUC contains 4 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 | 3-5 | 3 | 1 |
| α-helix | 8-17 | 10 | |
| β-strand | 22-28 | 7 | 1 |
| α-helix | 33-48 | 16 | |
| 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) |
>1AUC_1 THIOREDOXIN (chains A) MVKQIESKTAFQEALDAAGDKLVVVDFSATWCGPCKMIKPFFHSLSEKYSNVIFLEVDVD DCQDVASECEVKCMPTFQFFKKGQKVGEFSGANKEKLEATINELV
Human thioredoxin homodimers: regulation by pH, role of aspartate 60, and crystal structure of the aspartate 60 --> asparagine mutant. Andersen, J.F., Sanders, D.A., Gasdaska, J.R. et al. Biochemistry (1997) 36:13979-13988. DOI 10.1021/bi971004s · 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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