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Phosphoserine phosphatase

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Phosphoserine phosphatase (PSP) catalyzes the dephosphorylation of phosphoserine to produce serine and phosphate. This is the last reaction in serine biosynthesis. PSP is part of the glycine, serine and threonine metabolism. Mg+2 ion is a cofactor of PSP.

1 3D structures of phosphoserine phosphatase

3D structures of phosphoserine phosphatase

Updated on 02-September-2014

Phosphoserine phosphatase

2j70, 1w53 – BsPSP RsbT binding domain – Bacillus subtilis
2j6z, 2j6y - BsPSP RsbT binding domain (mutant)
4b6j – ToPSP – Thermococcus onnurineus
4ij5 – HtPSP – Hydrogenobacter thermophilus

Phosphoserine phosphatase binary complex

3p96 – PSP + Mg – Mycobacterium avium
3m1y – PSP + Mg – Helicobacter pylori
1l7o – MjPSP (mutant) + Zn – Methanocaldococcus jannaschii
1l8l – hPSP (mutant) + phosphono-propionic acid – human
1l8o – hPSP (mutant) + PO4
1nnl – hPSP + Ca
3w40, 3w41 – BsPSP + Mg
3w42, 3w43, 3w44 – BsPSP + Mn
3w45 – BsPSP + Co
4ap9 – ToPSP + pyridine derivative
4ij6 – HtPSP (mutant) + phosphoserine