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1W31

YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE 5-HYDROXYLAEVULINIC ACID COMPLEX

Summary for 1W31
Entry DOI10.2210/pdb1w31/pdb
Related1AW5 1EB3 1GJP 1H7N 1H7O 1H7P 1H7R 1OHL 1QML 1QNV 1YLV
DescriptorDELTA-AMINOLEVULINIC ACID DEHYDRATASE, 5-HYDROXYLAEVULINIC ACID, ZINC ION, ... (4 entities in total)
Functional Keywordsdehydratase, aldolase, tim barrel, tetrapyrrole synthesis, heme biosynthesis, lyase, zinc
Biological sourceSACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
Total number of polymer chains1
Total formula weight37968.70
Authors
Erskine, P.T.,Coates, L.,Newbold, R.,Brindley, A.A.,Stauffer, F.,Beaven, G.D.E.,Gill, R.,Wood, S.P.,Warren, M.J.,Cooper, J.B.,Shoolingin-Jordan, P.M.,Neier, R. (deposition date: 2004-07-11, release date: 2005-08-23, Last modification date: 2024-10-23)
Primary citationErskine, P.T.,Coates, L.,Newbold, R.,Brindley, A.A.,Stauffer, F.,Beaven, G.D.E.,Gill, R.,Coker, A.,Wood, S.P.,Warren, M.J.,Shoolingin-Jordan, P.M.,Neier, R.,Cooper, J.B.
Structure of Yeast 5-Aminolaevulinic Acid Dehydratase Complexed with the Inhibitor 5-Hydroxylaevulinic Acid
Acta Crystallogr.,Sect.D, 61:1222-, 2005
Cited by
PubMed Abstract: 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).
PubMed: 16131755
DOI: 10.1107/S0907444905018834
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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数据于2025-11-19公开中

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