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1f05
From Proteopedia
| 1f05, resolution 2.45Å () | |||||||||
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| Activity: | Transaldolase, with EC number 2.2.1.2 | ||||||||
| Domains: | Transaldolase_TalAB | ||||||||
| Related: | 1onr, 1ucw | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
CRYSTAL STRUCTURE OF HUMAN TRANSALDOLASE
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1F05 is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Thorell S, Gergely P Jr, Banki K, Perl A, Schneider G. The three-dimensional structure of human transaldolase. FEBS Lett. 2000 Jun 23;475(3):205-8. PMID:10869557
Page seeded by OCA on Mon Feb 16 22:40:05 2009
