1hbz
From Proteopedia
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|PDB= 1hbz |SIZE=350|CAPTION= <scene name='initialview01'>1hbz</scene>, resolution 1.50Å | |PDB= 1hbz |SIZE=350|CAPTION= <scene name='initialview01'>1hbz</scene>, resolution 1.50Å | ||
|SITE= <scene name='pdbsite=HEM:Hem+Binding+Site+For+Chain+A'>HEM</scene> | |SITE= <scene name='pdbsite=HEM:Hem+Binding+Site+For+Chain+A'>HEM</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Catalase Catalase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Catalase Catalase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hbz OCA], [http://www.ebi.ac.uk/pdbsum/1hbz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hbz RCSB]</span> | ||
}} | }} | ||
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[[Category: Murshudov, G N.]] | [[Category: Murshudov, G N.]] | ||
[[Category: Wilson, K S.]] | [[Category: Wilson, K S.]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: SO4]] | ||
[[Category: heme hydrogen peroxide]] | [[Category: heme hydrogen peroxide]] | ||
[[Category: iron]] | [[Category: iron]] | ||
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[[Category: peroxidase]] | [[Category: peroxidase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:01:55 2008'' |
Revision as of 18:01, 30 March 2008
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| , resolution 1.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Catalase, with EC number 1.11.1.6 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CATALASE FROM MICROCOCCUS LYSODEIKTICU
Overview
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.
About this Structure
1HBZ is a Single protein structure of sequence from Micrococcus luteus. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of catalase from Micrococcus lysodeikticus at 1.5 A resolution., Murshudov GN, Melik-Adamyan WR, Grebenko AI, Barynin VV, Vagin AA, Vainshtein BK, Dauter Z, Wilson KS, FEBS Lett. 1992 Nov 9;312(2-3):127-31. PMID:1426241
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