Structure analysis

Crystal structure of the catalytic domain of the heterodimeric human soluble guanylate cyclase 1.

X-ray diffraction
2.08Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero dimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero dimer

Binding statistics and energies are not available for this assembly
Assembly 2
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Multimeric state: hetero dimer
Accessible surface area: 16900 Å2
Buried surface area: 3200 Å2
Dissociation area: 1,300 Å2
Dissociation energy (ΔGdiss): 19 kcal/mol
Dissociation entropy (TΔSdiss): 12 kcal/mol
Interface energy (ΔGint): -24 kcal/mol
Symmetry number: 1

Macromolecules

Chains: A, C
Length: 225 amino acids
Theoretical weight: 24.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q02108 (Residues: 468-690; Coverage: 32%)
Gene names: GUC1A3, GUCSA3, GUCY1A1, GUCY1A3
Pfam: Adenylate and Guanylate cyclase catalytic domain
InterPro:
CATH: Nucleotide cyclase

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Chains: B, D
Length: 220 amino acids
Theoretical weight: 24.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q02153 (Residues: 408-619; Coverage: 34%)
Gene names: GUC1B3, GUCSB3, GUCY1B1, GUCY1B3
Pfam: Adenylate and Guanylate cyclase catalytic domain
InterPro:
CATH: Nucleotide cyclase

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