1SI8
Crystal structure of E. faecalis catalase
Summary for 1SI8
| Entry DOI | 10.2210/pdb1si8/pdb |
| Descriptor | Catalase, SULFATE ION, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | n-terminal arm; anti-parallel beta-barrel; wrapping region; c-terminal helical region; tetramer; heme group, oxidoreductase |
| Biological source | Enterococcus faecalis |
| Total number of polymer chains | 4 |
| Total formula weight | 222016.05 |
| Authors | Hakansson, K.O.,Brugna, M.,Tasse, L. (deposition date: 2004-02-28, release date: 2004-05-04, Last modification date: 2023-08-23) |
| Primary citation | Hakansson, K.O.,Brugna, M.,Tasse, L. The three-dimensional structure of catalase from Enterococcus faecalis. Acta Crystallogr.,Sect.D, 60:1374-1380, 2004 Cited by PubMed Abstract: Enterococcus faecalis haem catalase was crystallized using lithium sulfate at neutral pH. The crystals belong to space group R3, with unit-cell parameters a = b = 236.9, c = 198.1 A. The three-dimensional structure was determined by molecular replacement using a subunit of the Proteus mirabilis catalase structure. It was refined against 2.3 A synchrotron data to a free R factor of 21.8%. Like other catalases, the E. faecalis catalase is a homotetramer with a fold and structure similar to those of its structurally closest relative P. mirabilis. The solvent structure in the active site is identical in the four subunits but differs from that found in other catalases. The structural consequences of the Ramachandran outlier Ser196 are discussed. PubMed: 15272159DOI: 10.1107/S0907444904012004 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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