2FZN
Structure of the E. coli PutA proline dehydrogenase domain reduced by dithionite and complexed with proline
Summary for 2FZN
Entry DOI | 10.2210/pdb2fzn/pdb |
Descriptor | Bifunctional protein putA, Proline dehydrogenase (EC 1.5.99.8) (Proline oxidase), FLAVIN-ADENINE DINUCLEOTIDE, PROLINE, ... (4 entities in total) |
Functional Keywords | proline utilization a, proline dehydrogenase, puta, flavoenzyme, proline catabolism, dithionite-reduced, oxidoreductase |
Biological source | Escherichia coli |
Total number of polymer chains | 1 |
Total formula weight | 67568.75 |
Authors | Tanner, J.J. (deposition date: 2006-02-09, release date: 2006-12-26, Last modification date: 2023-08-30) |
Primary citation | Zhang, W.,Zhang, M.,Zhu, W.,Wanduragula, S.,Rewinkel, D.,Tanner, J.J.,Becker, D.F. Hydrogen Bonding Interactions of the 2-OH Ribityl Group and the N(5) Position of the FAD Cofactor Regulate PutA-membrane Associations in Escherichia coli To be Published, |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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