3D7J
SCO6650, a 6-pyruvoyltetrahydropterin synthase homolog from Streptomyces coelicolor
Summary for 3D7J
Entry DOI | 10.2210/pdb3d7j/pdb |
Descriptor | Uncharacterized protein SCO6650, SODIUM ION, CHLORIDE ION, ... (4 entities in total) |
Functional Keywords | t-fold, unknown function |
Biological source | Streptomyces coelicolor |
Total number of polymer chains | 6 |
Total formula weight | 100258.47 |
Authors | Spoonamore, J.E.,Roberts, S.A.,Heroux, A.,Bandarian, V. (deposition date: 2008-05-21, release date: 2008-10-21, Last modification date: 2024-10-30) |
Primary citation | Spoonamore, J.E.,Roberts, S.A.,Heroux, A.,Bandarian, V. Structure of a 6-pyruvoyltetrahydropterin synthase homolog from Streptomyces coelicolor. Acta Crystallogr.,Sect.F, 64:875-879, 2008 Cited by PubMed Abstract: The X-ray crystal structure of the 6-pyruvoyltetrahydropterin synthase (PTPS) homolog from Streptomyces coelicolor, SCO 6650, was solved at 1.5 A resolution. SCO 6650 forms a hexameric T-fold that closely resembles other PTPS proteins. The biological activity of SCO 6650 is unknown, but it lacks both a required active-site zinc metal ion and the essential catalytic triad and does not catalyze the PTPS reaction. However, SCO 6650 maintains active-site residues consistent with binding a pterin-like substrate. PubMed: 18931427DOI: 10.1107/S1744309108027048 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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