1HS6
STRUCTURE OF LEUKOTRIENE A4 HYDROLASE COMPLEXED WITH BESTATIN.
Summary for 1HS6
| Entry DOI | 10.2210/pdb1hs6/pdb |
| Descriptor | LEUKOTRIENE A-4 HYDROLASE, ZINC ION, YTTERBIUM (III) ION, ... (7 entities in total) |
| Functional Keywords | protein-inhibitor complex, alpha-beta protein, hydrolase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 70385.00 |
| Authors | Thunnissen, M.M.G.M.,Nordlund, P.N.,Haeggstrom, J.Z. (deposition date: 2000-12-24, release date: 2001-06-24, Last modification date: 2024-03-13) |
| Primary citation | Thunnissen, M.M.,Nordlund, P.,Haeggstrom, J.Z. Crystal structure of human leukotriene A(4) hydrolase, a bifunctional enzyme in inflammation. Nat.Struct.Biol., 8:131-135, 2001 Cited by PubMed Abstract: Leukotriene (LT) A(4) hydrolase/aminopeptidase (LTA4H) is a bifunctional zinc enzyme that catalyzes the biosynthesis of LTB4, a potent lipid chemoattractant involved in inflammation, immune responses, host defense against infection, and PAF-induced shock. The high resolution crystal structure of LTA4H in complex with the competitive inhibitor bestatin reveals a protein folded into three domains that together create a deep cleft harboring the catalytic Zn(2+) site. A bent and narrow pocket, shaped to accommodate the substrate LTA(4), constitutes a highly confined binding region that can be targeted in the design of specific anti-inflammatory agents. Moreover, the structure of the catalytic domain is very similar to that of thermolysin and provides detailed insight into mechanisms of catalysis, in particular the chemical strategy for the unique epoxide hydrolase reaction that generates LTB(4). PubMed: 11175901DOI: 10.1038/84117 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
Download full validation report
