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1f6k
From Proteopedia
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{{STRUCTURE_1f6k| PDB=1f6k | SCENE= }} | {{STRUCTURE_1f6k| PDB=1f6k | SCENE= }} | ||
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===CRYSTAL STRUCTURE ANALYSIS OF N-ACETYLNEURAMINATE LYASE FROM HAEMOPHILUS INFLUENZAE: CRYSTAL FORM II=== | ===CRYSTAL STRUCTURE ANALYSIS OF N-ACETYLNEURAMINATE LYASE FROM HAEMOPHILUS INFLUENZAE: CRYSTAL FORM II=== | ||
| + | {{ABSTRACT_PUBMED_11031117}} | ||
| - | + | ==Function== | |
| - | + | [[http://www.uniprot.org/uniprot/NANA_HAEIN NANA_HAEIN]] Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate. | |
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==About this Structure== | ==About this Structure== | ||
| - | + | [[1f6k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F6K OCA]. | |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:011031117</ref><references group="xtra"/><references/> |
[[Category: Haemophilus influenzae]] | [[Category: Haemophilus influenzae]] | ||
[[Category: N-acetylneuraminate lyase]] | [[Category: N-acetylneuraminate lyase]] | ||
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[[Category: Beta barrel]] | [[Category: Beta barrel]] | ||
[[Category: Lyase]] | [[Category: Lyase]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 15:31:19 2009'' | ||
Revision as of 11:02, 16 April 2014
Contents |
CRYSTAL STRUCTURE ANALYSIS OF N-ACETYLNEURAMINATE LYASE FROM HAEMOPHILUS INFLUENZAE: CRYSTAL FORM II
Template:ABSTRACT PUBMED 11031117
Function
[NANA_HAEIN] Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate.
About this Structure
1f6k is a 2 chain structure with sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.
Reference
- Barbosa JA, Smith BJ, DeGori R, Ooi HC, Marcuccio SM, Campi EM, Jackson WR, Brossmer R, Sommer M, Lawrence MC. Active site modulation in the N-acetylneuraminate lyase sub-family as revealed by the structure of the inhibitor-complexed Haemophilus influenzae enzyme. J Mol Biol. 2000 Oct 27;303(3):405-21. PMID:11031117 doi:http://dx.doi.org/10.1006/jmbi.2000.4138
