Chimeric GST Containing Inserts of Kininogen Peptides. Determined by X-ray diffraction at 2.2 Å resolution. Released 16 May 2012.
Explore 4ECC in 3D Show helices and sheets RCSB PDB PDBe
4ECC contains 8 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 |
| β-strand | 70-73 | 4 | 1 |
| β-strand | 76-79 | 4 | 1 |
| α-helix | 81-91 | 11 | |
| α-helix | 99-123 | 25 | |
| α-helix | 128-149 | 22 | |
| β-strand | 155 | 1 | 2 |
| β-strand | 158 | 1 | 2 |
| α-helix | 163-178 | 16 | |
| α-helix | 187-198 | 12 | |
| α-helix | 200-207 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| chimeric protein between GSHKT10 and domain 5 of kininogen-1 | A | protein | 231 | Schistosoma japonicum, homo sapiens | P01042 (AlphaFold model), P08515 (AlphaFold model) |
>4ECC_1 chimeric protein between GSHKT10 and domain 5 of kininogen-1 (chains A) MSPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELGKHGHGHGKHKN KGLEFPNLPYYIDGDVKLTQSMAIIRYIADKHNMLGGCPKERAEISMLEGAVLDIRYGVS RIAYSKDFETLKVDFLSKLPEMLKMFEDRLCHKTYLNGDHVTHPDFMLYDALDVVLYMDP MCLDAFPKLVCFKKRIEAIPQIDKYLKSSKYIAWPLQGWQATFGGGDHPPK
Chimeric glutathione S-transferases containing inserts of kininogen peptides: potential novel protein therapeutics. Bentley, A.A., Merkulov, S.M., Peng, Y. et al. J Biol Chem (2012) 287:22142-22150. DOI 10.1074/jbc.M112.372854 · PubMed
Other PDB entries of the same protein (UniProt P01042 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 4ECC directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.