1znc
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HUMAN CARBONIC ANHYDRASE IV
OverviewOverview
It has recently been demonstrated that the C-terminal deletion mutant of, recombinant human carbonic anhydrase IV (G267X CA IV) converts the, normally glycosylphosphatidylinositol-anchored enzyme into a soluble, secretory form which has the same catalytic properties as the, membrane-associated enzyme purified from human tissues. We have determined, the three-dimensional structure of the secretory form of human CA IV by, x-ray crystallographic methods to a resolution of 2.8 A. Although the zinc, binding site and the hydrophobic substrate binding pocket of CA IV are, generally similar to those of other mammalian isozymes, unique structural, differences are found elsewhere in the active site. Two disufide linkages, Cys-6-Cys-11G and Cys-23-Cys-203, stabilize the conformation of the, ... [(full description)]
About this StructureAbout this Structure
1ZNC is a [Single protein] structure of sequence from [Homo sapiens] with SO4 and ZN as [ligands]. Active as [[1]], with EC number [4.2.1.1]. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of the secretory form of membrane-associated human carbonic anhydrase IV at 2.8-A resolution., Stams T, Nair SK, Okuyama T, Waheed A, Sly WS, Christianson DW, Proc Natl Acad Sci U S A. 1996 Nov 26;93(24):13589-94. PMID:8942978
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