3E2S
Crystal Structure Reduced PutA86-630 Mutant Y540S Complexed with L-proline
Summary for 3E2S
Entry DOI | 10.2210/pdb3e2s/pdb |
Related | 1TIW 3E2Q 3E2S |
Descriptor | Proline dehydrogenase, PROLINE, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total) |
Functional Keywords | proline utilization a, puta, flavoenzyme, dna-binding, fad, flavoprotein, multifunctional enzyme, nad, oxidoreductase, proline metabolism, repressor, transcription, transcription regulation |
Biological source | Escherichia coli |
Total number of polymer chains | 1 |
Total formula weight | 62752.25 |
Authors | Tanner, J.J. (deposition date: 2008-08-06, release date: 2009-02-03, Last modification date: 2024-02-21) |
Primary citation | Ostrander, E.L.,Larson, J.D.,Schuermann, J.P.,Tanner, J.J. A conserved active site tyrosine residue of proline dehydrogenase helps enforce the preference for proline over hydroxyproline as the substrate. Biochemistry, 48:951-959, 2009 Cited by PubMed: 19140736DOI: 10.1021/bi802094k PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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