4UBP
STRUCTURE OF BACILLUS PASTEURII UREASE INHIBITED WITH ACETOHYDROXAMIC ACID AT 1.55 A RESOLUTION
Summary for 4UBP
| Entry DOI | 10.2210/pdb4ubp/pdb |
| Descriptor | PROTEIN (UREASE (CHAIN A)), PROTEIN (UREASE (CHAIN B)), PROTEIN (UREASE (CHAIN C)), ... (6 entities in total) |
| Functional Keywords | urease, bacillus pasteurii, nickel, acetohydroxamic acid, metalloenzyme, hydrolase |
| Biological source | Sporosarcina pasteurii More |
| Total number of polymer chains | 3 |
| Total formula weight | 87001.77 |
| Authors | Benini, S.,Rypniewski, W.R.,Wilson, K.S.,Ciurli, S.,Mangani, S. (deposition date: 1999-02-25, release date: 2000-03-06, Last modification date: 2023-11-15) |
| Primary citation | Benini, S.,Rypniewski, W.R.,Wilson, K.S.,Miletti, S.,Ciurli, S.,Mangani, S. The complex of Bacillus pasteurii urease with acetohydroxamate anion from X-ray data at 1.55 A resolution. J.Biol.Inorg.Chem., 5:110-118, 2000 Cited by PubMed Abstract: 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. PubMed: 10766443DOI: 10.1007/s007750050014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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