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
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Multimeric state: hetero dimer
Accessible surface area: 16827.6 Å2
Buried surface area: 3472.14 Å2
Dissociation area: 1,326.28 Å2
Dissociation energy (ΔGdiss): 16.51 kcal/mol
Dissociation entropy (TΔSdiss): 12.29 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-169668
Complex Portal ID: CPX-928
Assembly 2 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 16915.65 Å2
Buried surface area: 3182.4 Å2
Dissociation area: 1,337.98 Å2
Dissociation energy (ΔGdiss): 18.78 kcal/mol
Dissociation entropy (TΔSdiss): 12.27 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-169668
Complex Portal ID: CPX-928

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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