5IAT
Mechanistic and Structural Analysis of Substrate Recognition and Cofactor Binding by an Unusual Bacterial Prolyl Hydroxylase - apo-BaP4H
Summary for 5IAT
Entry DOI | 10.2210/pdb5iat/pdb |
Related | 5LAV 5LAX |
Descriptor | Procollagen-Proline Dioxygenase, GLYCEROL, DI(HYDROXYETHYL)ETHER, ... (4 entities in total) |
Functional Keywords | p4h, dioxygenase, cupin, fe(ii)/alpha-ketoglutarate, oxidoreductase |
Biological source | Bacillus anthracis |
Total number of polymer chains | 2 |
Total formula weight | 49813.61 |
Authors | Schnicker, N.J.,Dey, M. (deposition date: 2016-02-21, release date: 2016-04-27, Last modification date: 2023-09-27) |
Primary citation | Schnicker, N.J.,Dey, M. Bacillus anthracis Prolyl 4-Hydroxylase Modifies Collagen-like Substrates in Asymmetric Patterns. J.Biol.Chem., 291:13360-13374, 2016 Cited by PubMed: 27129244DOI: 10.1074/jbc.M116.725432 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.67 Å) |
Structure validation
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