PDBe 3uvj

X-ray diffraction
2.08Å resolution

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

Released:
Source organism: Homo sapiens

Function and Biology Details

Reaction catalysed:
GTP = 3',5'-cyclic GMP + diphosphate. 
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Guanylate cyclase soluble subunit beta-1 Chains: B, D
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:
  • Canonical: Q02153 (Residues: 408-619; Coverage: 34%)
Gene names: GUC1B3, GUCSB3, GUCY1B1, GUCY1B3
Sequence domains: Adenylate and Guanylate cyclase catalytic domain
Structure domains: Adenylyl Cyclase, chain A
Guanylate cyclase soluble subunit alpha-3 Chains: A, C
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:
  • Canonical: Q02108 (Residues: 468-690; Coverage: 32%)
Gene names: GUC1A3, GUCSA3, GUCY1A1, GUCY1A3
Sequence domains: Adenylate and Guanylate cyclase catalytic domain
Structure domains: Adenylyl Cyclase, chain A

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P21
Unit cell:
a: 50.78Å b: 139.1Å c: 55.46Å
α: 90° β: 91.47° γ: 90°
R-values:
R R work R free
0.214 0.167 0.209
Expression system: Escherichia coli BL21(DE3)