3CRT: PDB entry 3CRT

Structural characterization of an engineered allosteric protein. Determined by X-ray diffraction at 1.9 Å resolution. Released 24 Feb 2009.

Method
X-ray diffraction
Resolution
1.9 Å
Organism
Schistosoma japonicum
Chains
1
Atoms
1,938
Mol. weight
25.37 kDa
Ligands
GSH
Released
24 Feb 2009

Explore 3CRT in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 9 helices, 6 β-strands

ElementResiduesLengthSheet
β-strand4-851
α-helix12-143
α-helix15-239
β-strand29-3351
α-helix38-447
β-strand57-5931
β-strand64-6521
α-helix68-7811
α-helix86-10722
α-helix115-13622
β-strand14212
β-strand14512
α-helix150-16516
α-helix174-18512
α-helix187-1937

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Glutathione S-transferase class-mu 26 kDa isozymeAprotein214Schistosoma japonicumP08515 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3CRT_1 Glutathione S-transferase class-mu 26 kDa isozyme (chains A)
MSPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELGCEFPNLPYYID
GDVKLTQSMAIIRYIADKHNMLGGCPKERAEISMLEGAVLDIRYGVSRIAYSKDFETLKV
DFLSKLPEMLKMFEDRLCHKTYLNGDHVTHPDFMLYDALDVVLYMDPMCLDAFPKLVCFK
KRIEAIPQIDKYLKSSKYIAWPLQGWQATFGGGD

Ligands and cofactors

IDNameFormulaCopies
GSHGlutathioneC10 H17 N3 O6 S1

Primary citation

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:

Browse structure collections

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