› 1ykg

Solution NMR

Solution structure of the flavodoxin-like domain from the Escherichia coli sulfite reductase

Released:
DOI: 10.2210/pdb1ykg/pdb
PDB entry 1ykg coloured by chain, ensemble of 15 models, front view.
PDB entry 1ykg coloured by chain, ensemble of 15 models, side view.
PDB entry 1ykg coloured by chain, ensemble of 15 models, top view.
Source organism: Escherichia coli
Primary publication:
Solution structure of the sulfite reductase flavodoxin-like domain from Escherichia coli.
Sibille N, Blackledge M, Brutscher B, Covès J, Bersch B
Biochemistry 44 9086-95 (2005)
PMID: 15966732

Function and Biology Details

Reaction catalysed: 
H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3 NADPH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153532 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sulfite reductase [NADPH] flavoprotein alpha-component Chain: A
Molecule details ›
Chain: A
Length: 167 amino acids
Theoretical weight: 17.89 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P38038 (Residues: 53-219; Coverage: 28%)
Gene names: JW2734, b2764, cysJ
Sequence domains: Flavodoxin
Structure domains: Rossmann fold

Ligands and Environments


Cofactor: Ligand FMN 1 x FMN
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

2 review citations

The dual function of flavodiiron proteins: oxygen and/or nitric oxide reductases.
Romão et al. (2016)
1 more