1IHP
STRUCTURE OF PHOSPHOMONOESTERASE
Summary for 1IHP
| Entry DOI | 10.2210/pdb1ihp/pdb |
| Descriptor | PHYTASE, SULFATE ION (3 entities in total) |
| Functional Keywords | phosphomonoesterase, hydrolase, glycoprotein |
| Biological source | Aspergillus ficuum |
| Cellular location | Secreted: P34752 |
| Total number of polymer chains | 1 |
| Total formula weight | 48340.41 |
| Authors | Kostrewa, D. (deposition date: 1997-02-04, release date: 1998-03-18, Last modification date: 2024-10-09) |
| Primary citation | Kostrewa, D.,Gruninger-Leitch, F.,D'Arcy, A.,Broger, C.,Mitchell, D.,van Loon, A.P. Crystal structure of phytase from Aspergillus ficuum at 2.5 A resolution. Nat.Struct.Biol., 4:185-190, 1997 Cited by PubMed Abstract: 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. PubMed: 9164457DOI: 10.1038/nsb0397-185 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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