› 4ni2

X-ray diffraction
1.9Å resolution

Crystal structure of the heterodimeric catalytic domain of wild-type human soluble guanylate cyclase

Released:
DOI: 10.2210/pdb4ni2/pdb
PDB entry 4ni2 coloured by chain, front view.
PDB entry 4ni2 coloured by chain, side view.
PDB entry 4ni2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Interfacial residues promote an optimal alignment of the catalytic center in human soluble guanylate cyclase: heterodimerization is required but not sufficient for activity.
Seeger F, Quintyn R, Tanimoto A, Williams GJ, Tainer JA, Wysocki VH, Garcin ED
Biochemistry 53 2153-65 (2014)
PMID: 24669844

Function and Biology Details

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

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 Chain: A
Molecule details ›
Chain: A
Length: 197 amino acids
Theoretical weight: 21.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q02108 (Residues: 468-662; Coverage: 28%)
Gene names: GUC1A3, GUCSA3, GUCY1A1, GUCY1A3
Sequence domains: Adenylate and Guanylate cyclase catalytic domain
Structure domains: Nucleotide cyclase
Guanylate cyclase soluble subunit beta-1 Chain: B
Molecule details ›
Chain: B
Length: 209 amino acids
Theoretical weight: 23.57 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q02153 (Residues: 408-608; Coverage: 33%)
Gene names: GUC1B3, GUCSB3, GUCY1B1, GUCY1B3
Sequence domains: Adenylate and Guanylate cyclase catalytic domain
Structure domains: Nucleotide cyclase

Ligands and Environments

1 bound ligand:
Ligand EDO 6 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P212121
Unit cell:
a: 49.545Å b: 55.834Å c: 139.368Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.16 0.2
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

International Union of Basic and Clinical Pharmacology. CI. Structures and Small Molecule Modulators of Mammalian Adenylyl Cyclases.
Dessauer et al. (2017)
4 more

15 mentions without citation

Physiological activation and deactivation of soluble guanylate cyclase.
Horst et al. (2018)
14 more