Design of Disulfide-linked Thioredoxin Dimers and Multimers Through Analysis of Crystal Contacts. Determined by X-ray diffraction at 1.9 Å resolution. Released 11 Sept 2007.
Explore 2EIQ in 3D Show helices and sheets RCSB PDB PDBe
2EIQ contains 10 α-helices and 12 β-strands across 2 chains. 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 | 4-6 | 3 | 1 |
| α-helix | 7 | 1 | |
| α-helix | 9-11 | 3 | |
| β-strand | 12 | 1 | 2 |
| β-strand | 17 | 1 | 2 |
| β-strand | 22-28 | 7 | 1 |
| α-helix | 33-48 | 16 | |
| β-strand | 54-59 | 6 | 1 |
| α-helix | 66-69 | 4 | |
| β-strand | 77-82 | 6 | 1 |
| β-strand | 85-91 | 7 | 1 |
| α-helix | 96-106 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-6 | 3 | 3 |
| α-helix | 12 | 1 | |
| α-helix | 13-17 | 5 | |
| β-strand | 23-28 | 6 | 3 |
| α-helix | 33-48 | 16 | |
| β-strand | 54-59 | 6 | 3 |
| α-helix | 66-69 | 4 | |
| β-strand | 77-82 | 6 | 3 |
| β-strand | 85-91 | 7 | 3 |
| α-helix | 96-106 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Thioredoxin 1 | A, B | protein | 108 | Escherichia coli | P0AA25 (AlphaFold model) |
>2EIQ_1 Thioredoxin 1 (chains A, B) SDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNI DQNPGTAPKYGIRGIPTLLLFKNGEVAACKVGALSKGQLKEFLDANLA
| ID | Name | Formula | Copies |
|---|---|---|---|
| CU | Copper (II) ion | Cu | 2 |
Water and common crystallization additives (MPD) are not listed.
Design of Disulfide-linked Thioredoxin Dimers and Multimers Through Analysis of Crystal Contacts. Das, M., Kobayashi, M., Yamada, Y. et al. J Mol Biol (2007) 372:1278-1292. DOI 10.1016/j.jmb.2007.07.033 · PubMed
Other PDB entries of the same protein (UniProt P0AA25 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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