1rza
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X-RAY ANALYSIS OF METAL SUBSTITUTED HUMAN CARBONIC ANHYDRASE II DERIVATIVES
OverviewOverview
Metal-substituted crystals of human carbonic anhydrase II belonging to, space group P2(1) with cell dimensions a = 42.7, b = 41.7, c = 73.0 A and, beta = 104.6 degrees were analyzed crystallographically. The resolution, limit ranged from 1.82 to 1.92 A with high completeness (86.2-90.7%)., Cobalt(II)-substituted carbonic anhydrase has a tetrahedral coordination, around the metal both at pH 6 and pH 7.8, similar to the native zinc, enzyme. In contrast, the catalytically inactive copper(II), nickel(II) and, manganese(II) derivatives showed increased coordination number around the, metal ion. Whereas the copper is best described as penta-coordinated, the, nickel and manganese are best described as hexa-coordinated. The results, are briefly compared with spectroscopic observations and our current view, on carbonic anhydrase catalysis.
DiseaseDisease
Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[611492]
About this StructureAbout this Structure
1RZA is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Carbonate dehydratase, with EC number 4.2.1.1 Full crystallographic information is available from OCA.
ReferenceReference
X-ray analysis of metal-substituted human carbonic anhydrase II derivatives., Hakansson K, Wehnert A, Liljas A, Acta Crystallogr D Biol Crystallogr. 1994 Jan 1;50(Pt 1):93-100. PMID:15299481
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