1ho3
From Proteopedia
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|PDB= 1ho3 |SIZE=350|CAPTION= <scene name='initialview01'>1ho3</scene>, resolution 2.5Å | |PDB= 1ho3 |SIZE=350|CAPTION= <scene name='initialview01'>1ho3</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ASP:ASPARTIC ACID'>ASP</scene> | + | |LIGAND= <scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Asparaginase Asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.1 3.5.1.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Asparaginase Asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.1 3.5.1.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[3eca|3ECA]], [[4eca|4ECA]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ho3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ho3 OCA], [http://www.ebi.ac.uk/pdbsum/1ho3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ho3 RCSB]</span> | ||
}} | }} | ||
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[[Category: Palm, J G.]] | [[Category: Palm, J G.]] | ||
[[Category: Wlodawer, A.]] | [[Category: Wlodawer, A.]] | ||
| - | [[Category: ASP]] | ||
[[Category: asparaginase]] | [[Category: asparaginase]] | ||
[[Category: leukemia]] | [[Category: leukemia]] | ||
| - | ''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 21:08:14 2008'' |
Revision as of 18:08, 30 March 2008
| |||||||
| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Asparaginase, with EC number 3.5.1.1 | ||||||
| Related: | 3ECA, 4ECA
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE ANALYSIS OF E. COLI L-ASPARAGINASE II (Y25F MUTANT)
Overview
Quasi-enantiomorphic crystals of the Y25F mutant of Escherichia coli L-asparaginase and of the native Erwinia chrysanthemi L-asparaginase were obtained in the hexagonal space groups P6(5)22 and P6(1)22, respectively. The structures of these highly homologous enzymes were solved by molecular replacement and were refined with data extending to 2.2-2.5 A. These structures were compared with each other, as well as with other L-asparaginase structures previously observed with different crystal packing. It is concluded that the observed phenomenon, which is rare, was most likely to have arisen by chance.
About this Structure
1HO3 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structures of two highly homologous bacterial L-asparaginases: a case of enantiomorphic space groups., Jaskolski M, Kozak M, Lubkowski J, Palm G, Wlodawer A, Acta Crystallogr D Biol Crystallogr. 2001 Mar;57(Pt 3):369-77. PMID:11223513
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