Structural characterization of an engineered allosteric protein. Determined by X-ray diffraction at 1.9 Å resolution. Released 24 Feb 2009.
Explore 3CRT in 3D Show helices and sheets RCSB PDB PDBe
3CRT contains 9 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 | 4-8 | 5 | 1 |
| α-helix | 12-14 | 3 | |
| α-helix | 15-23 | 9 | |
| β-strand | 29-33 | 5 | 1 |
| α-helix | 38-44 | 7 | |
| β-strand | 57-59 | 3 | 1 |
| β-strand | 64-65 | 2 | 1 |
| α-helix | 68-78 | 11 | |
| α-helix | 86-107 | 22 | |
| α-helix | 115-136 | 22 | |
| β-strand | 142 | 1 | 2 |
| β-strand | 145 | 1 | 2 |
| α-helix | 150-165 | 16 | |
| α-helix | 174-185 | 12 | |
| α-helix | 187-193 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glutathione S-transferase class-mu 26 kDa isozyme | A | protein | 214 | Schistosoma japonicum | P08515 (AlphaFold model) |
>3CRT_1 Glutathione S-transferase class-mu 26 kDa isozyme (chains A) MSPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELGCEFPNLPYYID GDVKLTQSMAIIRYIADKHNMLGGCPKERAEISMLEGAVLDIRYGVSRIAYSKDFETLKV DFLSKLPEMLKMFEDRLCHKTYLNGDHVTHPDFMLYDALDVVLYMDPMCLDAFPKLVCFK KRIEAIPQIDKYLKSSKYIAWPLQGWQATFGGGD
| ID | Name | Formula | Copies |
|---|---|---|---|
| GSH | Glutathione | C10 H17 N3 O6 S | 1 |
Using affinity chromatography to engineer and characterize pH-dependent protein switches. Sagermann, M., Chapleau, R.R., DeLorimier, E. et al. Protein Sci (2009) 18:217-228. DOI 10.1002/pro.23 · PubMed
Other PDB entries of the same protein (UniProt P08515 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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