3d5y: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:3d5y.png|left|200px]] | [[Image:3d5y.png|left|200px]] | ||
{{STRUCTURE_3d5y| PDB=3d5y | SCENE= }} | {{STRUCTURE_3d5y| PDB=3d5y | SCENE= }} | ||
===High resolution crystal structure of 1,5-alpha-arabinanase catalytic mutant (AbnBE201A)=== | ===High resolution crystal structure of 1,5-alpha-arabinanase catalytic mutant (AbnBE201A)=== | ||
{{ABSTRACT_PUBMED_19505290}} | {{ABSTRACT_PUBMED_19505290}} | ||
==About this Structure== | ==About this Structure== | ||
[[3d5y]] is a 1 chain structure of [[Arabinanase]] with sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D5Y OCA]. | |||
==See Also== | |||
*[[Arabinanase|Arabinanase]] | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:019505290</ref><references group="xtra"/> | ||
[[Category: Arabinan endo-1,5-alpha-L-arabinosidase]] | [[Category: Arabinan endo-1,5-alpha-L-arabinosidase]] | ||
[[Category: Geobacillus stearothermophilus]] | [[Category: Geobacillus stearothermophilus]] | ||
| Line 35: | Line 26: | ||
[[Category: Glycosyl hydrolase]] | [[Category: Glycosyl hydrolase]] | ||
[[Category: High resolution]] | [[Category: High resolution]] | ||
[[Category: Hydrolase]] | |||
Revision as of 11:25, 27 July 2012
High resolution crystal structure of 1,5-alpha-arabinanase catalytic mutant (AbnBE201A)
Template:ABSTRACT PUBMED 19505290
About this Structure
3d5y is a 1 chain structure of Arabinanase with sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.
See Also
Reference
- Alhassid A, Ben-David A, Tabachnikov O, Libster D, Naveh E, Zolotnitsky G, Shoham Y, Shoham G. Crystal structure of an inverting GH 43 1,5-alpha-L-arabinanase from Geobacillus stearothermophilus complexed with its substrate. Biochem J. 2009 Jul 29;422(1):73-82. PMID:19505290 doi:10.1042/BJ20090180