X-ray diffraction
1.46Å resolution

Structure of proline utilization A with cis-4-hydroxy-D-proline bound in the L-glutamate-gamma-semialdehyde dehydrogenase active site


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:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Bifunctional protein PutA Chains: A, B
Molecule details ›
Chains: A, B
Length: 1235 amino acids
Theoretical weight: 131.96 KDa
Source organism: Sinorhizobium meliloti SM11
Expression system: Escherichia coli
  • Canonical: F7X6I3 (Residues: 1-1233; Coverage: 100%)
Gene names: SM11_chr0102, putA
Sequence domains:

Ligands and Environments

Cofactor: Ligand FAD 2 x FAD

Cofactor: Ligand NAD 2 x NAD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P21
Unit cell:
a: 100.89Å b: 101.92Å c: 126.2Å
α: 90° β: 106.44° γ: 90°
R R work R free
0.195 0.194 0.22
Expression system: Escherichia coli