1mku: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 20: Line 20:


==About this Structure==
==About this Structure==
1MKU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MKU OCA].  
1MKU is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MKU OCA].  


==Reference==
==Reference==
Phospholipase A2 engineering. Structural and functional roles of the highly conserved active site residue aspartate-99., Sekar K, Yu BZ, Rogers J, Lutton J, Liu X, Chen X, Tsai MD, Jain MK, Sundaralingam M, Biochemistry. 1997 Mar 18;36(11):3104-14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9115986 9115986]
<ref group="xtra">PMID:9115986</ref><references group="xtra"/>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Sundaralingam, M.]]
[[Category: Sundaralingam, M.]]
[[Category: Carboxylic ester hydrolase]]
[[Category: Carboxylic ester hydrolase]]
Line 32: Line 31:
[[Category: Orthorhombic form]]
[[Category: Orthorhombic form]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul  3 00:12:50 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 17:29:50 2009''

Revision as of 18:29, 17 February 2009

File:1mku.png

Template:STRUCTURE 1mku

CARBOXYLIC ESTER HYDROLASE, ORTHORHOMBIC FORM OF THE TRIPLE MUTANTCARBOXYLIC ESTER HYDROLASE, ORTHORHOMBIC FORM OF THE TRIPLE MUTANT

Template:ABSTRACT PUBMED 9115986

About this StructureAbout this Structure

1MKU is a 1 chain structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. Sekar K, Yu BZ, Rogers J, Lutton J, Liu X, Chen X, Tsai MD, Jain MK, Sundaralingam M. Phospholipase A2 engineering. Structural and functional roles of the highly conserved active site residue aspartate-99. Biochemistry. 1997 Mar 18;36(11):3104-14. PMID:9115986 doi:10.1021/bi961576x

Page seeded by OCA on Tue Feb 17 17:29:50 2009

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA