1czr

X-ray diffraction
1.9Å resolution

COMPARISONS OF WILD TYPE AND MUTANT FLAVODOXINS FROM ANACYSTIS NIDULANS. STRUCTURAL DETERMINANTS OF THE REDOX POTENTIALS.

Released:

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Flavodoxin Chain: A
Molecule details ›
Chain: A
Length: 169 amino acids
Theoretical weight: 18.66 KDa
Source organism: Synechococcus elongatus PCC 7942
Expression system: Escherichia coli
UniProt:
  • Canonical: P10340 (Residues: 2-170; Coverage: 99%)
Gene names: Synpcc7942_1541, isiB
Sequence domains: Flavodoxin
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 60.03Å b: 65.77Å c: 51.43Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.154 0.154 0.193
Expression system: Escherichia coli