1ihp

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STRUCTURE OF PHOSPHOMONOESTERASE

Structural highlights

1ihp is a 1 chain structure with sequence from Aspergillus ficuum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:SO4
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PHYA_ASPNG Catalyzes the hydrolysis of inorganic orthophosphate from phytate.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Phytase is a high molecular weight acid phosphatase. The structure has an alpha/beta-domain similar to that of rat acid phosphatase and an alpha-domain with a new fold.

Crystal structure of phytase from Aspergillus ficuum at 2.5 A resolution.,Kostrewa D, Gruninger-Leitch F, D'Arcy A, Broger C, Mitchell D, van Loon AP Nat Struct Biol. 1997 Mar;4(3):185-90. PMID:9164457[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
14 reviews cite this structure
Reduction of phytic acid and enhancement of bioavailable micronutrients in food grains.
Gupta et al. (2015)
13 more
52 other articles
No citations found

See Also

References

  1. ↑ Kostrewa D, Gruninger-Leitch F, D'Arcy A, Broger C, Mitchell D, van Loon AP. Crystal structure of phytase from Aspergillus ficuum at 2.5 A resolution. Nat Struct Biol. 1997 Mar;4(3):185-90. PMID:9164457

Contents


PDB ID 1ihp

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OCA

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