We've built a new version of this page with an interactive 3D viewer. Try it out in beta and help us improve:

› 8uq0

X-ray diffraction
1.43Å resolution

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

Released:
DOI: 10.2210/pdb8uq0/pdb
Model geometry
Fit model/data
PDB entry 8uq0 coloured by chain, front view.
PDB entry 8uq0 coloured by chain, side view.
PDB entry 8uq0 coloured by chain, top view.
Source organism: Sinorhizobium meliloti SM11
Primary publication:
Noncovalent Inhibition and Covalent Inactivation of Proline Dehydrogenase by Analogs of N-Propargylglycine.
Tanner JJ, Ji J, Bogner AN, Scott GK, Patel SM, Seravalli J, Gates KS, Benz CC, Becker DF
Biochemistry (2024)
PMID: 39437336

Function and Biology Details

Reactions catalysed: 
L-glutamate 5-semialdehyde + NAD(+) + H2O = L-glutamate + NADH + 2 H(+).
L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a quinol + H(+).
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: 26-81, 191-522; Coverage: 32%)
Gene names: SM11_chr0102, putA
Sequence domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
2 bound ligands:
Ligand X7K 2 x X7K
Ligand PEG 1 x PEG
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P1
Unit cell:
a: 48.839Å b: 55.098Å c: 75.911Å
α: 103.95° β: 100.55° γ: 108.41°
R-values:
R R work R free
0.162 0.161 0.183
Expression system: Escherichia coli

Quick links