4IOT
High-resolution Structure of Triosephosphate isomerase from E. coli
Summary for 4IOT
Entry DOI | 10.2210/pdb4iot/pdb |
Descriptor | Triosephosphate isomerase, SULFATE ION (3 entities in total) |
Functional Keywords | structural genomics, montreal-kingston bacterial structural genomics initiative, bsgi, tim barrel, conversion of dihydroxyacetone phosphate to d-glyceraldehyde-3-phosphate, cytosol, isomerase |
Biological source | Escherichia coli |
Cellular location | Cytoplasm (By similarity): B1XB85 |
Total number of polymer chains | 2 |
Total formula weight | 54103.67 |
Authors | Vinaik, R.,Kozlov, G.,Gehring, K.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (deposition date: 2013-01-08, release date: 2013-01-23, Last modification date: 2023-09-20) |
Primary citation | Kozlov, G.,Vinaik, R.,Gehring, K. Triosephosphate isomerase is a common crystallization contaminant of soluble His-tagged proteins produced in Escherichia coli. Acta Crystallogr.,Sect.F, 69:499-502, 2013 Cited by PubMed: 23695562DOI: 10.1107/S1744309113010841 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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