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1zs9

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==About this Structure==
==About this Structure==
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1ZS9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1wdh 1wdh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZS9 OCA].
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1ZS9 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1wdh 1wdh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZS9 OCA].
==Reference==
==Reference==
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Crystal structure of human E1 enzyme and its complex with a substrate analog reveals the mechanism of its phosphatase/enolase activity., Wang H, Pang H, Bartlam M, Rao Z, J Mol Biol. 2005 May 13;348(4):917-26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15843022 15843022]
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<ref group="xtra">PMID:15843022</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
 
[[Category: Bartlam, M.]]
[[Category: Bartlam, M.]]
[[Category: Pang, H.]]
[[Category: Pang, H.]]
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[[Category: Structure human enolase-phosphatase e1]]
[[Category: Structure human enolase-phosphatase e1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:00:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 11:49:41 2009''

Revision as of 09:49, 17 February 2009

Image:1zs9.png

Template:STRUCTURE 1zs9

Crystal structure of human enolase-phosphatase E1

Template:ABSTRACT PUBMED 15843022

About this Structure

1ZS9 is a 1 chain structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1wdh. Full crystallographic information is available from OCA.

Reference

  • Wang H, Pang H, Bartlam M, Rao Z. Crystal structure of human E1 enzyme and its complex with a substrate analog reveals the mechanism of its phosphatase/enolase activity. J Mol Biol. 2005 May 13;348(4):917-26. PMID:15843022 doi:10.1016/j.jmb.2005.01.072

Page seeded by OCA on Tue Feb 17 11:49:41 2009

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