Function and Biology Details
Reaction catalysed:
GTP = 3',5'-cyclic GMP + diphosphate
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169668 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Guanylate cyclase soluble subunit alpha-1
Molecule details ›
Chains: A, C
Length: 225 amino acids
Theoretical weight: 24.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Adenylate and Guanylate cyclase catalytic domain
Structure domains: Nucleotide cyclase
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%)
Sequence domains: Adenylate and Guanylate cyclase catalytic domain
Structure domains: Nucleotide cyclase
Guanylate cyclase soluble subunit beta-1
Molecule details ›
Chains: B, D
Length: 220 amino acids
Theoretical weight: 24.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Adenylate and Guanylate cyclase catalytic domain
Structure domains: Nucleotide cyclase
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%)
Sequence domains: Adenylate and Guanylate cyclase catalytic domain
Structure domains: Nucleotide cyclase
