2fw4 | pdb_00002fw4

Carbonic anhydrase activators. The first X-ray crystallographic study of an activator of isoform I, structure with L-histidine.

spinqualitylabelsall models 2fw4, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2fw4 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HIS, ZN Activity: Carbonate dehydratase, with EC number 4.2.1.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CAH1_HUMAN] Reversible hydration of carbon dioxide. Can hydrates cyanamide to urea. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The X-ray crystallographic structure for the adduct of an activator with human carbonic anhydrase isozyme I (hCA I) is reported. L-Histidine binds deep within the enzyme active site, participating in a network of hydrogen bonds involving its carboxylate moiety and the zinc-bound water molecule, as well as the imidazole of His200, being in van der Waals contacts with Thr199, His200, His64, and His67. This binding is very different from that to the other major cytosolic isozyme hCA II. Carbonic anhydrase activators: the first X-ray crystallographic study of an adduct of isoform I.,Temperini C, Scozzafava A, Supuran CT Bioorg Med Chem Lett. 2006 Oct 1;16(19):5152-6. Epub 2006 Jul 25. PMID:16870440 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Carbonic anhydrase 3D structures

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