1f05
CRYSTAL STRUCTURE OF HUMAN TRANSALDOLASE
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| , resolution 2.45Å | |||||||
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| Activity: | Transaldolase, with EC number 2.2.1.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Leukemia-1, T-cell acute lymphocytic OMIM:[187040], Transaldolase deficiency OMIM:[602063]
About this StructureAbout this Structure
1F05 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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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