1raz: Difference between revisions
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==Overview== | ==Overview== | ||
The three-dimensional structure of human carbonic anhydrase II complexed | The three-dimensional structure of human carbonic anhydrase II complexed with azide and with bromide was investigated crystallographically. Both of these non-protonated inhibitors replace the zinc and the 'deep' water, two catalytically important water molecules in the active site of the molecule. Both the azide and the bromide ions bind in a distorted tetrahedral manner 0.4 and 1.1 A from the zinc water position, respectively, but are in close contact (2.0 and 2.6 A, respectively) with the zinc ion. | ||
==Disease== | ==Disease== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Hakansson, K.]] | [[Category: Hakansson, K.]] | ||
[[Category: Jonsson, B | [[Category: Jonsson, B M.]] | ||
[[Category: Liljas, A.]] | [[Category: Liljas, A.]] | ||
[[Category: BR]] | [[Category: BR]] | ||
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[[Category: lyase(oxo-acid)]] | [[Category: lyase(oxo-acid)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:48:59 2008'' | ||
Revision as of 15:49, 21 February 2008
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THE STRUCTURE OF HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH BROMIDE AND AZIDE
OverviewOverview
The three-dimensional structure of human carbonic anhydrase II complexed with azide and with bromide was investigated crystallographically. Both of these non-protonated inhibitors replace the zinc and the 'deep' water, two catalytically important water molecules in the active site of the molecule. Both the azide and the bromide ions bind in a distorted tetrahedral manner 0.4 and 1.1 A from the zinc water position, respectively, but are in close contact (2.0 and 2.6 A, respectively) with the zinc ion.
DiseaseDisease
Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[611492]
About this StructureAbout this Structure
1RAZ 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
The structure of human carbonic anhydrase II in complex with bromide and azide., Jonsson BM, Hakansson K, Liljas A, FEBS Lett. 1993 May 10;322(2):186-90. PMID:8482389
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