Brand  (β version)

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information
centroid:
interaction residue:

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Ligands
Code Name Link
FDA Dihydroflavine-adenine dinucleotide
Modified Residues
Code Name Link
LYX N''-(2-coenzyme a)-propanoyl-lysine
Code : 3ITG
Header : OXIDOREDUCTASE
Title : Structure the proline utilization A proline dehydrogenase domain (PutA86-630) inactivated with N-propargylglycine
Release Data : 2010-01-12
Compound :
mol_id molecule chains synonym
1 Bifunctional protein putA A,B Proline dehydrogenase, Proline oxidase, Delta-1-pyrroline-5-carboxylate dehydrogenase, P5C dehydrogenase
ec: 1.5.99.8, 1.5.1.12
fragment: Proline dehydrogenase domain, residues 86-630
Source :
mol_id organism_scientific expression_system
1 Escherichia coli K-12  (taxid:83333) Escherichia coli  (taxid:562)
strain: K12
gene: putA, poaA, b1014, JW0999
expression_system_strain: BL21(DE3) pLysS
expression_system_vector_type: plasmid
expression_system_plasmid: pET23b
Authors : Tanner, J.J.
Keywords : Proline utilization A, PutA, flavoenzyme, mechanism-based inactivation, DNA-binding, FAD, Flavoprotein, Multifunctional enzyme, NAD, Oxidoreductase, Proline metabolism, Repressor, Transcription, Transcription regulation
Exp. method : X-RAY DIFFRACTION ( 2.150 Å )
Citation :

The structure of the proline utilization a proline dehydrogenase domain inactivated by N-propargylglycine provides insight into conformational changes induced by substrate binding and flavin reduction.

Srivastava, D.,Zhu, W.,Johnson, W.H.  et al.
(2010)  Biochemistry  49 : 560 - 569

PubMed: 19994913
DOI: 10.1021/bi901717s

Chain : A, B
UniProt : P09546 (PUTA_ECOLI)
Reaction : L-proline + a quinone = (S)-1-pyrroline-5- carboxylate + a quinol.
L-glutamate 5-semialdehyde + NAD(+) + H(2)O = L-glutamate + NADH.