4hmx

X-ray diffraction
1.59Å resolution

Crystal structure of PhzG from Burkholderia lata 383 in complex with tetrahydrophenazine-1-carboxylic acid

Released:

Function and Biology Details

Reaction catalysed:
(1R)-1,4,5,10-tetrahydrophenazine-1-carboxylate + O(2) = (10aS)-5,10-dihydrophenazine-1-carboxylate + H(2)O(2)
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-174461 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrophenazinedicarboxylate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 215 amino acids
Theoretical weight: 24.22 KDa
Source organism: Burkholderia lata
Expression system: Escherichia coli
UniProt:
  • Canonical: Q396C5 (Residues: 1-212; Coverage: 100%)
Gene names: Bcep18194_B1572, phzG
Sequence domains:
Structure domains: Electron Transport, Fmn-binding Protein; Chain A

Ligands and Environments


Cofactor: Ligand FMN 2 x FMN
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P31
Unit cell:
a: 93.65Å b: 93.65Å c: 51.41Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.115 0.113 0.158
Expression system: Escherichia coli