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Structure paper

TitleInterfacial residues promote an optimal alignment of the catalytic center in human soluble guanylate cyclase: heterodimerization is required but not sufficient for activity.
Journal, issue, pagesBiochemistry, Vol. 53, Page 2153-2165, Year 2014
Publish dateNov 5, 2013 (structure data deposition date)
AuthorsSeeger, F. / Quintyn, R. / Tanimoto, A. / Williams, G.J. / Tainer, J.A. / Wysocki, V.H. / Garcin, E.D.
External linksBiochemistry / PubMed:24669844
MethodsX-ray diffraction
Resolution1.9 Å
Structure data

PDB-4ni2:
Crystal structure of the heterodimeric catalytic domain of wild-type human soluble guanylate cyclase
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsLYASE / heterodimeric / cGMP biosynthesis / nitric oxide / cyclase / GTP-binding / metal-binding / nucleotide binding / CYTOSOL

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