1f05
From Proteopedia
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| - | [[Image:1f05.gif|left|200px]] | + | [[Image:1f05.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF HUMAN TRANSALDOLASE''' | + | {{Structure |
| + | |PDB= 1f05 |SIZE=350|CAPTION= <scene name='initialview01'>1f05</scene>, resolution 2.45Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Transaldolase Transaldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.2 2.2.1.2] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF HUMAN TRANSALDOLASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1F05 is a [ | + | 1F05 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F05 OCA]. |
==Reference== | ==Reference== | ||
| - | The three-dimensional structure of human transaldolase., Thorell S, Gergely P Jr, Banki K, Perl A, Schneider G, FEBS Lett. 2000 Jun 23;475(3):205-8. PMID:[http:// | + | The three-dimensional structure of human transaldolase., Thorell S, Gergely P Jr, Banki K, Perl A, Schneider G, FEBS Lett. 2000 Jun 23;475(3):205-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10869557 10869557] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: alpha-beta barrel]] | [[Category: alpha-beta barrel]] | ||
| - | ''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 11:02:35 2008'' |
Revision as of 09:02, 20 March 2008
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| , resolution 2.45Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Transaldolase, with EC number 2.2.1.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF HUMAN TRANSALDOLASE
Contents |
Overview
The crystal structure of human transaldolase has been determined to 2.45 A resolution. The enzyme folds into an alpha/beta barrel structure and is thus similar in structure to other class I aldolases. Structure-based sequence alignment of available sequences of the transaldolase subfamily reveals that eight active site residues are invariant in the whole subfamily. Other invariant residues are mainly involved in the formation of the hydrophobic core of the enzyme. Noteworthy is a hydrophobic cluster consisting of five invariant residues. Human transaldolase has been implicated as an autoantigen in multiple sclerosis and four immunodominant peptide segments are located at the surface of the enzyme, accessible to autoantibodies.
Disease
Known diseases associated with this structure: Leukemia-1, T-cell acute lymphocytic OMIM:[187040], Transaldolase deficiency OMIM:[602063]
About this Structure
1F05 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of human transaldolase., Thorell S, Gergely P Jr, Banki K, Perl A, Schneider G, FEBS Lett. 2000 Jun 23;475(3):205-8. PMID:10869557
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