1jeh
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1jeh |SIZE=350|CAPTION= <scene name='initialview01'>1jeh</scene>, resolution 2.40Å | |PDB= 1jeh |SIZE=350|CAPTION= <scene name='initialview01'>1jeh</scene>, resolution 2.40Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene> | + | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Dihydrolipoyl_dehydrogenase Dihydrolipoyl dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.4 1.8.1.4] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyl_dehydrogenase Dihydrolipoyl dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.4 1.8.1.4] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jeh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jeh OCA], [http://www.ebi.ac.uk/pdbsum/1jeh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jeh RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Takenaka, A.]] | [[Category: Takenaka, A.]] | ||
[[Category: Toyoda, T.]] | [[Category: Toyoda, T.]] | ||
| - | [[Category: FAD]] | ||
[[Category: 2-oxoglutarate dehydrogenase complex]] | [[Category: 2-oxoglutarate dehydrogenase complex]] | ||
[[Category: pyruvate dehydrogenase complex]] | [[Category: pyruvate dehydrogenase complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:32:30 2008'' |
Revision as of 18:32, 30 March 2008
| |||||||
| , resolution 2.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Dihydrolipoyl dehydrogenase, with EC number 1.8.1.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF YEAST E3, LIPOAMIDE DEHYDROGENASE
Overview
The crystal structure of eucaryotic lipoamide dehydrogenase from yeast has been determined by an X-ray analysis at 2.7 (partially at 2.4) A resolution. The enzyme has two identical subunits related by a pseudo twofold symmetry. The tertiary structure is similar to those of other procaryotic enzymes. The active site, consisting of FAD, Cys44, and Cys49 from one subunit and His457' from the other subunit, is highly conserved. This enzyme is directly bound to the core protein E2 of the 2-oxoglutarate dehydrogenase complex, whereas it is bound to the pyruvate dehydrogenase complex through a protein X. The calculated electrostatic potential suggests two characteristic regions for binding with these two proteins.
About this Structure
1JEH is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structure of eucaryotic E3, lipoamide dehydrogenase from yeast., Toyoda T, Suzuki K, Sekiguchi T, Reed LJ, Takenaka A, J Biochem. 1998 Apr;123(4):668-74. PMID:9538259
Page seeded by OCA on Sun Mar 30 21:32:30 2008
