Phosphoserine phosphatase

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<applet load='1l8o' size='400' frame='true' align='right' caption='Phosphoserine phosphatase dimer complex with phosphate [[1l8o]]' />
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<applet load='1l8o' size='400' frame='true' align='right' caption='Phosphoserine phosphatase dimer complex with phosphoserine [[1l8o]]' />

Revision as of 09:12, 30 December 2013

Phosphoserine phosphatase dimer complex with phosphoserine 1l8o

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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.

3D structures of phosphoserine phosphatase

2j70, 1w53 – BsPSP RsbT binding domain – Bacillus subtilis
2j6z, 2j6y - BsPSP RsbT binding domain (mutant)

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

Phosphoserine phosphatase ternary complex

1f5s, 1j97, 1l7m – MjPSP + PO4 + Mg
1l7n – MjPSP + AlF4 + Mg
1l7p – MjPSP (mutant) + phosphoserine + PO4

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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