1XHK
Crystal structure of M. jannaschii Lon proteolytic domain
Summary for 1XHK
Entry DOI | 10.2210/pdb1xhk/pdb |
Descriptor | Putative protease La homolog, SULFATE ION, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (4 entities in total) |
Functional Keywords | lon protease, protease la, atp dependent, catalytic dyad, hydrolase |
Biological source | Methanocaldococcus jannaschii |
Cellular location | Cell membrane (By similarity); Multi-pass membrane protein (Potential): Q58812 |
Total number of polymer chains | 2 |
Total formula weight | 40683.63 |
Authors | Im, Y.J.,Na, Y.,Kang, G.B.,Rho, S.-H.,Kim, M.-K.,Lee, J.H.,Chung, C.H.,Eom, S.H. (deposition date: 2004-09-20, release date: 2004-10-05, Last modification date: 2011-07-13) |
Primary citation | Im, Y.J.,Na, Y.,Kang, G.B.,Rho, S.H.,Kim, M.K.,Lee, J.H.,Chung, C.H.,Eom, S.H. The active site of a lon protease from Methanococcus jannaschii distinctly differs from the canonical catalytic Dyad of Lon proteases. J.Biol.Chem., 279:53451-53457, 2004 Cited by PubMed: 15456757DOI: 10.1074/jbc.M410437200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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