1ex5: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1ex5.gif|left|200px]] | [[Image:1ex5.gif|left|200px]] | ||
'''FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE''' | {{Structure | ||
|PDB= 1ex5 |SIZE=350|CAPTION= <scene name='initialview01'>1ex5</scene>, resolution 2.2Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13] | |||
|GENE= | |||
}} | |||
'''FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1EX5 is a [ | 1EX5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EX5 OCA]. | ||
==Reference== | ==Reference== | ||
A conserved glutamate residue exhibits multifunctional catalytic roles in D-fructose-1,6-bisphosphate aldolases., Maurady A, Zdanov A, de Moissac D, Beaudry D, Sygusch J, J Biol Chem. 2002 Mar 15;277(11):9474-83. Epub 2002 Jan 4. PMID:[http:// | A conserved glutamate residue exhibits multifunctional catalytic roles in D-fructose-1,6-bisphosphate aldolases., Maurady A, Zdanov A, de Moissac D, Beaudry D, Sygusch J, J Biol Chem. 2002 Mar 15;277(11):9474-83. Epub 2002 Jan 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11779856 11779856] | ||
[[Category: Fructose-bisphosphate aldolase]] | [[Category: Fructose-bisphosphate aldolase]] | ||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
| Line 21: | Line 30: | ||
[[Category: schiff base]] | [[Category: schiff base]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:01:25 2008'' | ||