1HBZ
Catalase from Micrococcus lysodeikticu
Summary for 1HBZ
| Entry DOI | 10.2210/pdb1hbz/pdb |
| Descriptor | CATALASE, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | oxidoreductase, peroxidase, iron, heme hydrogen peroxide |
| Biological source | MICROCOCCUS LYSODEIKTICUS |
| Total number of polymer chains | 1 |
| Total formula weight | 57019.43 |
| Authors | Murshudov, G.N.,Grebenko, A.I.,Barynin, V.V.,Braningen, J.,Wilson, K.S.,Dauter, Z.,Melik-Adamyan, W.R. (deposition date: 2001-04-24, release date: 2001-05-24, Last modification date: 2024-05-08) |
| Primary citation | Murshudov, G.N.,Melik-Adamyan, W.R.,Grebenko, A.I.,Barynin, V.V.,Vagin, A.A.,Vainshtein, B.K.,Dauter, Z.,Wilson, K.S. Three-Dimensional Structure of Catalase from Micrococcus Lysodeikticus at 1.5A Resolution FEBS Lett., 312:127-, 1992 Cited by PubMed Abstract: The three-dimensional crystal structure of catalase from Micrococcus lysodeikticus has been solved by multiple isomorphous replacement and refined at 1.5 A resolution. The subunit of the tetrameric molecule of 222 symmetry consists of a single polypeptide chain of about 500 amino acid residues and one haem group. The crystals belong to space group P4(2)2(1)2 with unit cell parameters a = b = 106.7 A, c = 106.3 A, and there is one subunit of the tetramer per asymmetric unit. The amino acid sequence has been tentatively determined by computer graphics model building and comparison with the known three-dimensional structure of beef liver catalase and sequences of several other catalases. The atomic model has been refined by Hendrickson and Konnert's least-squares minimisation against 94,315 reflections between 8 A and 1.5 A. The final model consists of 3,977 non-hydrogen atoms of the protein and haem group, 426 water molecules and one sulphate ion. The secondary and tertiary structures of the bacterial catalase have been analyzed and a comparison with the structure of beef liver catalase has been made. PubMed: 1426241DOI: 10.1016/0014-5793(92)80919-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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