4kbp
From Proteopedia
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[[Category: purple acid phosphatase]] | [[Category: purple acid phosphatase]] | ||
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Revision as of 15:43, 30 October 2007
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KIDNEY BEAN PURPLE ACID PHOSPHATASE
Overview
Purple acid phosphatase is a widely distributed non-specific, phosphomonoesterase. X-ray structures of the dimeric 111-kDa, Fe(III)-Zn(II) kidney bean purple acid phosphatase (kbPAP) complexed with, phosphate, the product of the reaction, and with tungstate, a strong, inhibitor of the phosphatase activity, were determined at 2.7 and 3.0, angstroms resolution, respectively. Furthermore the resolution of the, unligated enzyme, recently solved at 2.9 angstroms could be extended to, 2.65 angstroms with completely new data. The binding of both oxoanions is, not accompanied by larger conformational changes in the enzyme structure., Small movements with a maximal coordinate shift of 1 angstroms are only, observed for the active site residues His295 and His296. In the inhibitor, complex as well ... [(full description)]
About this Structure
4KBP is a [Single protein] structure of sequence from [Phaseolus vulgaris] with NAG, FE, ZN and PO4 as [ligands]. Active as [Acid phosphatase], with EC number [3.1.3.2]. Structure known Active Sites: ACA, ACB, ACC and ACD. Full crystallographic information is available from [OCA].
Reference
Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures., Klabunde T, Strater N, Frohlich R, Witzel H, Krebs B, J Mol Biol. 1996 Jun 21;259(4):737-48. PMID:8683579
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