7E6J
Aspartyl/Asparaginyl beta-hydroxylase (AspH) H725A in complex with Factor X peptide fragment (39mer-4Ser)
Summary for 7E6J
| Entry DOI | 10.2210/pdb7e6j/pdb |
| Descriptor | Aspartyl/asparaginyl beta-hydroxylase, Peptide from Factor X light chain, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | aspartyl/asparaginyl beta-hydroxylase, dioxygenase, oxidoreductase |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 53879.01 |
| Authors | Nakashima, Y.,Brasnett, A.,Brewitz, L.,Schofield, C.J. (deposition date: 2021-02-22, release date: 2021-06-30, Last modification date: 2024-11-20) |
| Primary citation | Brasnett, A.,Pfeffer, I.,Brewitz, L.,Chowdhury, R.,Nakashima, Y.,Tumber, A.,McDonough, M.A.,Schofield, C.J. Human Oxygenase Variants Employing a Single Protein Fe II Ligand Are Catalytically Active. Angew.Chem.Int.Ed.Engl., 60:14657-14663, 2021 Cited by PubMed Abstract: Aspartate/asparagine-β-hydroxylase (AspH) is a human 2-oxoglutarate (2OG) and Fe oxygenase that catalyses C3 hydroxylations of aspartate/asparagine residues of epidermal growth factor-like domains (EGFDs). Unusually, AspH employs two histidine residues to chelate Fe rather than the typical triad of two histidine and one glutamate/aspartate residue. We report kinetic, inhibition, and crystallographic studies concerning human AspH variants in which either of its Fe binding histidine residues are substituted for alanine. Both the H725A and, in particular, the H679A AspH variants retain substantial catalytic activity. Crystal structures clearly reveal metal-ligation by only a single protein histidine ligand. The results have implications for the functional assignment of 2OG oxygenases and for the design of non-protein biomimetic catalysts. PubMed: 33887099DOI: 10.1002/anie.202103711 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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