 |
PDBe Entry: 1tj0 
Crystal structure of E. coli PutA proline dehydrogenase domain (residues 86-669) co-crystallized with L-lactate
 |
OXIDOREDUCTASE
|
|
X-RAY DIFFRACTION
|
|
Resolution: 2.1 Å, R-factor: 21.4%, Free R-factor: 25.855%, Spacegroup: I 2 2 2
|
|
26/10/2004, deposition: 02/06/2004, last revision: 24/02/2009
|
|
Tanner, J.J.; Zhang, M.; White, T.A.; Schuermann, J.P.; Baban, B.A.; Becker, D.F.
|
Structures of the Escherichia coli PutA proline dehydrogenase domain in complex with competitive inhibitors
BIOCHEMISTRY vol:43, pag:12539-12548 (2004) [PubMed ID 15449943 ]
|
|
beta/alpha barrel, flavoenzyme, FAD, proline catabolism, L-lactate, OXIDOREDUCTASE
|
|
1.5.1.12 ExPASy BRENDA 1.5.99.8 ExPASy BRENDA (A)
|
|
Escherichia coli 562(A)
|
|
Bifunctional protein putA [Includes: Proline dehydrogenase (EC 1.5.99.8) (Proline oxidase); Delta-1-pyrroline-5-carboxylate dehydrogenase (EC 1.5.1.12) (P5C dehydrogenase)] P09546 (A)
|
|
A
|
|
1tiw, 1tj1, 1tj2
|
| A |
Bifunctional putA protein |
Protein |
P09546 (PUTA_ECOLI)
|
602 |
77% |
|
| A |
FLAVIN-ADENINE DINUCLEOTIDE |
FAD
|
| A |
LACTIC ACID |
LAC
|
|
|
