Structure analysis

Structural basis of the improvement of ChrR - a multi-purpose enzyme

X-ray diffraction
2.2Å resolution
Source organism: Escherichia coli K-12
Assemblies composition:
homo tetramer
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1
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Multimeric state: homo tetramer
Accessible surface area: 26056.54 Å2
Buried surface area: 12538.81 Å2
Dissociation area: 1,603.69 Å2
Dissociation energy (ΔGdiss): 8.44 kcal/mol
Dissociation entropy (TΔSdiss): 13.82 kcal/mol
Symmetry number: 4
PDBe Complex ID: PDB-CPX-142829
Assembly 2 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 14617.98 Å2
Buried surface area: 4682.2 Å2
Dissociation area: 1,603.5 Å2
Dissociation energy (ΔGdiss): 11.88 kcal/mol
Dissociation entropy (TΔSdiss): 12.56 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-142828

Macromolecules

Chains: A, B
Length: 193 amino acids
Theoretical weight: 20.85 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AGE6 (Residues: 1-188; Coverage: 100%)
Gene names: JW3691, b3713, chrR, yieF
Pfam: NADPH-dependent FMN reductase
InterPro:
CATH: Rossmann fold

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