4ubp
From Proteopedia
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STRUCTURE OF BACILLUS PASTEURII UREASE INHIBITED WITH ACETOHYDROXAMIC ACID AT 1.55 A RESOLUTION
Overview
The structure of Bacillus pasteurii urease inhibited with acetohydroxamic, acid was solved and refined anisotropically using synchrotron X-ray, cryogenic diffraction data (1.55 A resolution, 99.5% completeness, data, redundancy = 26, R-factor = 15.1%, PDB code 4UBP). The two Ni ions in the, active site are separated by a distance of 3.53 A. The structure clearly, shows the binding mode of the inhibitor anion, symmetrically bridging the, two Ni ions in the active site through the hydroxamate oxygen and, chelating one Ni ion through the carbonyl oxygen. The flexible flap, flanking the active site cavity is in the open conformation. The possible, implications of the results on structure-based molecular design of new, urease inhibitors are discussed.
About this Structure
4UBP is a Protein complex structure of sequences from Sporosarcina pasteurii with NI, ACE and HAE as ligands. Active as Urease, with EC number 3.5.1.5 Full crystallographic information is available from OCA.
Reference
The complex of Bacillus pasteurii urease with acetohydroxamate anion from X-ray data at 1.55 A resolution., Benini S, Rypniewski WR, Wilson KS, Miletti S, Ciurli S, Mangani S, J Biol Inorg Chem. 2000 Feb;5(1):110-8. PMID:10766443
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