3B7U
Leukotriene A4 Hydrolase Complexed with KELatorphan
Summary for 3B7U
| Entry DOI | 10.2210/pdb3b7u/pdb |
| Related | 2R59 3B7R 3B7S 3B7T |
| Descriptor | Leukotriene A-4 hydrolase, ZINC ION, YTTERBIUM (III) ION, ... (7 entities in total) |
| Functional Keywords | transition state, analogue peptide, hydrolysis, alternative splicing, cytoplasm, hydrolase, leukotriene biosynthesis, metal-binding, metalloprotease, multifunctional enzyme, protease, zinc |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 71069.62 |
| Authors | Tholander, F.,Haeggstrom, J.,Thunnissen, M.,Muroya, A.,Roques, B.-P.,Fournie-Zaluski, M.-C. (deposition date: 2007-10-31, release date: 2008-09-16, Last modification date: 2023-08-30) |
| Primary citation | Tholander, F.,Muroya, A.,Roques, B.P.,Fournie-Zaluski, M.C.,Thunnissen, M.M.,Haeggstrom, J.Z. Structure-based dissection of the active site chemistry of leukotriene a4 hydrolase: implications for m1 aminopeptidases and inhibitor design. Chem.Biol., 15:920-929, 2008 Cited by PubMed Abstract: M1 aminopeptidases comprise a large family of biologically important zinc enzymes. We show that peptide turnover by the M1 prototype, leukotriene A4 hydrolase/aminopeptidase, involves a shift in substrate position associated with exchange of zinc coordinating groups, while maintaining the overall coordination geometry. The transition state is stabilized by residues conserved among M1 members and in the final reaction step, Glu-296 of the canonical zinc binding HEXXH motif shuffles a proton from the hydrolytic water to the leaving group. Tripeptide substrates bind along the conserved GXMEN motif, precisely occupying the distance between Glu-271 and Arg-563, whereas the Arg specificity is governed by a narrow S1 pocket capped with Asp-375. Our data provide detailed insights to the active site chemistry of M1 aminopeptidases and will aid in the development of novel enzyme inhibitors. PubMed: 18804029DOI: 10.1016/j.chembiol.2008.07.018 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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