4op9 | pdb_00004op9

Urate OXIDASE IN COMPLEX WITH 8-AZAXANTHINE

spinqualitylabelsall models 4op9, resolution 1.58Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4op9 is a 1 chain structure with sequence from Aspfl. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AZA, NA NonStd Res: ACE Related: 4op6 Gene: uaZ, uox (ASPFL) Activity: Factor independent urate hydroxylase, with EC number 1.7.3.3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [URIC_ASPFL] Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin. Publication Abstract from PubMed Urate oxidase from Aspergillus flavus is a 135 kDa homo-tetramer which has a hydrophobic cavity buried within each monomer and located close to its active site. Crystallographic studies under moderate gas pressure and high hydrostatic pressure have shown that both gas presence and high pressure would rigidify the cavity leading to an inhibition of the catalytic activity. Analysis of the cavity volume variations and functional modifications suggest that the flexibility of the cavity would be an essential parameter for the active site efficiency. This cavity would act as a connecting vessel to give flexibility to the neighboring active site, and its expansion under pure oxygen pressure reveals that it might serve as a transient reservoir on its pathway to the active site. Functional relevance of the internal hydrophobic cavity of urate oxidase.,Colloc'h N, Prange T FEBS Lett. 2014 May 2;588(9):1715-9. doi: 10.1016/j.febslet.2014.03.017. Epub, 2014 Mar 18. PMID:24657440 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Urate Oxidase

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