1w31
From Proteopedia
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| , resolution 1.9Å | |||||||
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| Sites: | |||||||
| Ligands: | and | ||||||
| Activity: | Porphobilinogen synthase, with EC number 4.2.1.24 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE 5-HYDROXYLAEVULINIC ACID COMPLEX
Overview
The X-ray structure of the enzyme 5-aminolaevulinic acid dehydratase (ALAD) from yeast complexed with the competitive inhibitor 5-hydroxylaevulinic acid has been determined at a resolution of 1.9 A. The structure shows that the inhibitor is bound by a Schiff-base link to one of the invariant active-site lysine residues (Lys263). The inhibitor appears to bind in two well defined conformations and the interactions made by it suggest that it is a very close analogue of the substrate 5-aminolaevulinic acid (ALA).
About this Structure
1W31 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structure of yeast 5-aminolaevulinic acid dehydratase complexed with the inhibitor 5-hydroxylaevulinic acid., Erskine PT, Coates L, Newbold R, Brindley AA, Stauffer F, Beaven GD, Gill R, Coker A, Wood SP, Warren MJ, Shoolingin-Jordan PM, Neier R, Cooper JB, Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1222-6. Epub 2005, Aug 16. PMID:16131755
Page seeded by OCA on Thu Mar 20 14:51:26 2008
Categories: Porphobilinogen synthase | Saccharomyces cerevisiae | Single protein | Beaven, G D.E. | Brindley, A A. | Coates, L. | Cooper, J B. | Erskine, P T. | Gill, R. | Neier, R. | Newbold, R. | Shoolingin-Jordan, P M. | Stauffer, F. | Warren, M J. | Wood, S P. | SHO | ZN | Aldolase | Dehydratase | Heme biosynthesis | Lyase | Tetrapyrrole synthesis | Tim barrel | Zinc
