5TI8
Crystal Structure of an aspartate aminotransferase from Pseudomonas
Summary for 5TI8
| Entry DOI | 10.2210/pdb5ti8/pdb |
| Descriptor | Aminotransferase, CALCIUM ION (3 entities in total) |
| Functional Keywords | aminotransferase, transferase |
| Biological source | Pseudomonas sp. (strain M1) |
| Total number of polymer chains | 2 |
| Total formula weight | 104927.75 |
| Authors | Peat, T.S.,Newman, J. (deposition date: 2016-10-01, release date: 2017-01-11, Last modification date: 2023-10-04) |
| Primary citation | Wilding, M.,Scott, C.,Newman, J.,Peat, T.S. Crystal structure of a putrescine aminotransferase from Pseudomonas sp. strain AAC. Acta Crystallogr F Struct Biol Commun, 73:29-35, 2017 Cited by PubMed Abstract: The putrescine aminotransferase KES24511 from Pseudomonas sp. strain AAC was previously identified as an industrially relevant enzyme based on the discovery that it is able to promiscuously catalyse the transamination of 12-aminododecanoic acid. Here, the cloning, heterologous expression, purification and successful crystallization of the KES24511 protein are reported, which ultimately generated crystals adopting space group I2. The crystals diffracted X-rays to 2.07 Å resolution and data were collected using the microfocus beamline of the Australian Synchrotron. The structure was solved using molecular replacement, with a monomer from PDB entry 4a6t as the search model. PubMed: 28045391DOI: 10.1107/S2053230X16019658 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.07 Å) |
Structure validation
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