Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:1.45
Classification:UNKNOWN FUNCTION
Release Date:2008-10-21
Deposition Date:2008-05-21
Revision Date:2011-07-13#2012-03-28
Molecular Weight:100258.47
Macromolecule Type:Protein
Residue Count:912
Atom Site Count:6349
DOI:10.2210/pdb3d7j/pdb
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.
Resolution:1.45
Classification:UNKNOWN FUNCTION
Release Date:2008-10-21
Deposition Date:2008-05-21
Revision Date:2011-07-13#2012-03-28
Molecular Weight:100258.47
Macromolecule Type:Protein
Residue Count:912
Atom Site Count:6349
DOI:10.2210/pdb3d7j/pdb
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.
| Date made available | 2008 |
|---|---|
| Publisher | RCSB-PDB |