5UR2
Crystal structure of proline utilization A (PutA) from Bdellovibrio bacteriovorus inactivated by N-propargylglycine
Summary for 5UR2
Entry DOI | 10.2210/pdb5ur2/pdb |
Descriptor | Bifunctional protein PutA, N-propargylglycine-modified flavin adenine dinucleotide (3 entities in total) |
Functional Keywords | flavoenzyme, rossmann fold, aldehyde dehydrogenase, flavin adenine dinucleotide, nicotinamide adenine dinucleotide, proline catabolism, substrate channeling, bifunctional enzyme, mechanism-based inactivation, oxidoreductase |
Biological source | Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100) |
Total number of polymer chains | 4 |
Total formula weight | 442146.84 |
Authors | Tanner, J.J. (deposition date: 2017-02-09, release date: 2017-08-02, Last modification date: 2023-10-04) |
Primary citation | Korasick, D.A.,Singh, H.,Pemberton, T.A.,Luo, M.,Dhatwalia, R.,Tanner, J.J. Biophysical investigation of type A PutAs reveals a conserved core oligomeric structure. FEBS J., 284:3029-3049, 2017 Cited by PubMed: 28710792DOI: 10.1111/febs.14165 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.23 Å) |
Structure validation
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