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-Structure paper
Title | The phosphoglycerate kinase 1 variants found in carcinoma cells display different catalytic activity and conformational stability compared to the native enzyme. |
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Journal, issue, pages | PLoS ONE, Vol. 13, Page e0199191-e0199191, Year 2018 |
Publish date | Oct 10, 2016 (structure data deposition date) |
![]() | Fiorillo, A. / Petrosino, M. / Ilari, A. / Pasquo, A. / Cipollone, A. / Maggi, M. / Chiaraluce, R. / Consalvi, V. |
![]() | ![]() ![]() |
Methods | X-ray diffraction |
Resolution | 1.64 - 2.05 Å |
Structure data | ![]() PDB-5m1r: ![]() PDB-5m3u: ![]() PDB-5m6z: ![]() PDB-5mxm: ![]() PDB-5o7d: |
Chemicals | ![]() ChemComp-ADP: ![]() ChemComp-MG: ![]() ChemComp-HOH: ![]() ChemComp-3PG: ![]() ChemComp-PO4: ![]() ChemComp-BTB: |
Source |
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![]() | TRANSFERASE / Phosphoglycerate kinase / Single Nucleotide Polymorphism derived mutant G166D / human V216F phosphoglycerate kinase 1 mutant / human phosphoglycerate kinase 1 / M189I SNP -derived mutant |