1hfk: Difference between revisions

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[[Image:1hfk.gif|left|200px]]<br /><applet load="1hfk" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1hfk.gif|left|200px]]
caption="1hfk, resolution 2.17&Aring;" />
 
'''ASPARAGINASE FROM ERWINIA CHRYSANTHEMI, HEXAGONAL FORM WITH WEAK SULFATE'''<br />
{{Structure
|PDB= 1hfk |SIZE=350|CAPTION= <scene name='initialview01'>1hfk</scene>, resolution 2.17&Aring;
|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>
|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]
|GENE=
}}
 
'''ASPARAGINASE FROM ERWINIA CHRYSANTHEMI, HEXAGONAL FORM WITH WEAK SULFATE'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1HFK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Known structural/functional Sites: <scene name='pdbsite=AS1:Active+Site+Chain+A'>AS1</scene> and <scene name='pdbsite=AS2:Active+Site+Chain+C'>AS2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HFK OCA].  
1HFK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HFK OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11223513 11223513]
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:[http://www.ncbi.nlm.nih.gov/pubmed/11223513 11223513]
[[Category: Asparaginase]]
[[Category: Asparaginase]]
[[Category: Erwinia chrysanthemi]]
[[Category: Erwinia chrysanthemi]]
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[[Category: hydrolase]]
[[Category: hydrolase]]


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Revision as of 12:36, 20 March 2008

File:1hfk.gif


PDB ID 1hfk

Drag the structure with the mouse to rotate
, resolution 2.17Å
Sites: and
Ligands:
Activity: Asparaginase, with EC number 3.5.1.1
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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