Assemblies
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
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
Macromolecules
Chains: A, C
Length: 225 amino acids
Theoretical weight: 24.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Pfam: Adenylate and Guanylate cyclase catalytic domain
InterPro:
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%)
Pfam: Adenylate and Guanylate cyclase catalytic domain
InterPro:
- Adenylyl cyclase class-3/4/guanylyl cyclase
- Nucleotide cyclase
- Adenylyl cyclase class-4/guanylyl cyclase, conserved site
Chains: B, D
Length: 220 amino acids
Theoretical weight: 24.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Pfam: Adenylate and Guanylate cyclase catalytic domain
InterPro:
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%)
Pfam: Adenylate and Guanylate cyclase catalytic domain
InterPro:
- Adenylyl cyclase class-3/4/guanylyl cyclase
- Nucleotide cyclase
- Adenylyl cyclase class-4/guanylyl cyclase, conserved site