Structure analysis

Crystal structure of an H-NOX protein from S. oneidensis in the Fe(II)CO ligation state, Q154A/Q155A/K156A mutant

X-ray diffraction
2.25Å resolution
Source organism: Shewanella oneidensis MR-1
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 9800 Å2
Buried surface area: 1600 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Interface energy (ΔGint): -37 kcal/mol
Symmetry number: 1
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 9700 Å2
Buried surface area: 1300 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Interface energy (ΔGint): -26 kcal/mol
Symmetry number: 1

Macromolecules

Chains: A, B
Length: 187 amino acids
Theoretical weight: 21.16 KDa
Source organism: Shewanella oneidensis MR-1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8EF49 (Residues: 1-181; Coverage: 100%)
Gene name: SO_2144
Pfam: Haem-NO-binding
InterPro:
CATH: H-NOX domain

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