3K5T
Crystal structure of human diamine oxidase in space group C2221
Summary for 3K5T
| Entry DOI | 10.2210/pdb3k5t/pdb |
| Descriptor | Diamine oxidase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, COPPER (II) ION, ... (7 entities in total) |
| Functional Keywords | oxidoreductase, copper amine oxidase, cao, topaquinone, tpq, diamine oxidase, dao, human, glycoprotein, heparin-binding, metal-binding, secreted |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 84769.60 |
| Authors | McGrath, A.P.,Guss, J.M. (deposition date: 2009-10-08, release date: 2010-02-09, Last modification date: 2023-09-06) |
| Primary citation | McGrath, A.P.,Hilmer, K.M.,Collyer, C.A.,Dooley, D.M.,Guss, J.M. A new crystal form of human diamine oxidase. Acta Crystallogr.,Sect.F, 66:137-142, 2010 Cited by PubMed Abstract: Copper amine oxidases (CAOs) are ubiquitous in nature and catalyse the oxidative deamination of primary amines to the corresponding aldehydes. Humans have three viable CAO genes (AOC1-3). AOC1 encodes human diamine oxidase (hDAO), which is the frontline enzyme for histamine metabolism. hDAO is unique among CAOs in that it has a distinct substrate preference for diamines. The structure of hDAO in space group P2(1)2(1)2(1) with two molecules in the asymmetric unit has recently been reported. Here, the structure of hDAO refined to 2.1 A resolution in space group C222(1) with one molecule in the asymmetric unit is reported. PubMed: 20124708DOI: 10.1107/S1744309109052130 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.11 Å) |
Structure validation
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