› 8dkq

X-ray diffraction
1.72Å resolution

Minimal PutA proline dehydrogenase domain (design #2) complexed with 2-(Furan-2-yl)acetic acid

Released:
DOI: 10.2210/pdb8dkq/pdb
PDB entry 8dkq coloured by chain, front view.
PDB entry 8dkq coloured by chain, side view.
PDB entry 8dkq coloured by chain, top view.
Source organism: Sinorhizobium meliloti SM11
Primary publication:
Structure-based engineering of minimal Proline dehydrogenase domains for inhibitor discovery.
Bogner AN, Ji J, Tanner JJ
Protein Eng Des Sel (2022)
PMID: 36448708

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
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123683 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional protein PutA Chains: A, B
Molecule details ›
Chains: A, B
Length: 396 amino acids
Theoretical weight: 43.77 KDa
Source organism: Sinorhizobium meliloti SM11
Expression system: Escherichia coli
UniProt:
  • Canonical: F7X6I3 (Residues: 26-83, 190-522; Coverage: 32%)
Gene names: SM11_chr0102, putA
Sequence domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
2 bound ligands:
Ligand SJU 2 x SJU
Ligand PEG 1 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P1
Unit cell:
a: 48.967Å b: 55.291Å c: 76.092Å
α: 104.07° β: 100.37° γ: 108.67°
R-values:
R R work R free
0.168 0.166 0.196
Expression system: Escherichia coli

Quick links

Citations

1 mention without citation

Structure-based engineering of minimal proline dehydrogenase domains for inhibitor discovery.
Bogner et al. (2022)