1tj1

X-ray diffraction
2Å resolution

Crystal structure of E. coli PutA proline dehydrogenase domain (residues 86-669) complexed with L-lactate

Released:

Function and Biology Details

Reactions catalysed:
L-glutamate 5-semialdehyde + NAD(+) + H(2)O = L-glutamate + NADH
L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a quinol
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
PDBe Complex ID:
PDB-CPX-140693 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional protein PutA Chain: A
Molecule details ›
Chain: A
Length: 602 amino acids
Theoretical weight: 66.67 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P09546 (Residues: 86-669; Coverage: 44%)
Gene names: JW0999, b1014, poaA, putA
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: I222
Unit cell:
a: 72.814Å b: 141.124Å c: 146.015Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.214 0.255
Expression system: Escherichia coli