1hfk: Difference between revisions
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|PDB= 1hfk |SIZE=350|CAPTION= <scene name='initialview01'>1hfk</scene>, resolution 2.17Å | |PDB= 1hfk |SIZE=350|CAPTION= <scene name='initialview01'>1hfk</scene>, resolution 2.17Å | ||
|SITE= <scene name='pdbsite=AS1:Active+Site+Chain+A'>AS1</scene> and <scene name='pdbsite=AS2:Active+Site+Chain+C'>AS2</scene> | |SITE= <scene name='pdbsite=AS1:Active+Site+Chain+A'>AS1</scene> and <scene name='pdbsite=AS2:Active+Site+Chain+C'>AS2</scene> | ||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hfk OCA], [http://www.ebi.ac.uk/pdbsum/1hfk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hfk RCSB]</span> | |||
}} | }} | ||
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[[Category: Palm, G J.]] | [[Category: Palm, G J.]] | ||
[[Category: Wlodawer, A.]] | [[Category: Wlodawer, A.]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
''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 21:04:12 2008'' | ||
Revision as of 21:04, 30 March 2008
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| , resolution 2.17Å | |||||||
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| Sites: | and | ||||||
| Ligands: | |||||||
| Activity: | Asparaginase, with EC number 3.5.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ASPARAGINASE FROM ERWINIA CHRYSANTHEMI, HEXAGONAL FORM WITH WEAK SULFATE
OverviewOverview
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 StructureAbout this Structure
1HFK is a Single protein structure of sequence from Erwinia chrysanthemi. Full crystallographic information is available from OCA.
ReferenceReference
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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