› 4pu0

X-ray diffraction
2.3Å resolution

Crystal structure of the Escherichia coli alkanesulfonate FMN reductase SsuE in FMNH2-bound form

Released:
DOI: 10.2210/pdb4pu0/pdb
PDB entry 4pu0 coloured by chain, front view.
PDB entry 4pu0 coloured by chain, side view.
PDB entry 4pu0 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Crystal structure of Escherichia coli SsuE: defining a general catalytic cycle for FMN reductases of the flavodoxin-like superfamily.
Driggers CM, Dayal PV, Ellis HR, Karplus PA
Biochemistry 53 3509-19 (2014)
PMID: 24816272

Function and Biology Details

Reaction catalysed: 
FMNH(2) + NADP(+) = FMN + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160439 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FMN reductase (NADPH) Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 191 amino acids
Theoretical weight: 21.28 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P80644 (Residues: 1-191; Coverage: 100%)
Gene names: JW0920, b0937, ssuE, ycbP
Sequence domains: NADPH-dependent FMN reductase
Structure domains: Rossmann fold

Ligands and Environments


Cofactor: Ligand FMN 3 x FMN
2 bound ligands:
Ligand GOL 3 x GOL
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: P6122
Unit cell:
a: 187.018Å b: 187.018Å c: 91.336Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.176 0.174 0.221
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Assessing and maximizing data quality in macromolecular crystallography.
Karplus et al. (2015)
7 other articles

3 mentions without citation

Not as easy as π: An insertional residue does not explain the π-helix gain-of-function in two-component FMN reductases.
McFarlane et al. (2019)
2 more