Structure of proline utilization A with the FAD covalently modified by L-thiazolidine-2-carboxylate

Covalent Modification of the Flavin in Proline Dehydrogenase by Thiazolidine-2-Carboxylate.

20% PEG-3350, 0.2M AMMONIUM SULFATE,
REMARK 280 0.1M MGCL2, 0.1M HEPES, 0.1M NA FORMATE, 10MM NAD+, 50MM thiazolidine-2-carboxylate, PH 8.0

National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)

Bifunctional protein PutA (E.C.1.5.5.2,1.2.1.88)
FLAVOENZYME, ROSSMANN FOLD, PROLINE CATABOLISM, SUBSTRATE CHANNELING, BIFUNCTIONAL ENZYME, OXIDOREDUCTASE
binding site for residues FAD A 1301 and T2C A 1304
binding site for residues FAD B 1301 and T2C B 1304