1RZD

X-RAY ANALYSIS OF METAL SUBSTITUTED HUMAN CARBONIC ANHYDRASE II DERIVATIVES

Summary for 1RZD

• Entry DOI: 10.2210/pdb1rzd/pdb
• Descriptor: CARBONIC ANHYDRASE II, MANGANESE (II) ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: lyase(oxo-acid)
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm : P00918
• Total number of polymer chains: 1
• Total formula weight: 29308.86

Authors

Hakansson, K.,Wehnert, A.,Liljas, A. (deposition date: 1993-05-25, release date: 1993-10-31, Last modification date: 2024-02-14)

Primary citation

Hakansson, K.,Wehnert, A.,Liljas, A.
X-ray analysis of metal-substituted human carbonic anhydrase II derivatives.
Acta Crystallogr.,Sect.D, 50:93-100, 1994

PubMed Abstract: 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.

PubMed: 15299481
DOI: 10.1107/S0907444993008790

Experimental method

X-RAY DIFFRACTION (1.9 Å)