1w31
From Proteopedia
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|PDB= 1w31 |SIZE=350|CAPTION= <scene name='initialview01'>1w31</scene>, resolution 1.9Å | |PDB= 1w31 |SIZE=350|CAPTION= <scene name='initialview01'>1w31</scene>, resolution 1.9Å | ||
|SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=SHO:5-HYDROXYLAEVULINIC+ACID'>SHO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Porphobilinogen_synthase Porphobilinogen synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.24 4.2.1.24] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Porphobilinogen_synthase Porphobilinogen synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.24 4.2.1.24] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w31 OCA], [http://www.ebi.ac.uk/pdbsum/1w31 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w31 RCSB]</span> | ||
}} | }} | ||
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[[Category: Warren, M J.]] | [[Category: Warren, M J.]] | ||
[[Category: Wood, S P.]] | [[Category: Wood, S P.]] | ||
| - | [[Category: SHO]] | ||
| - | [[Category: ZN]] | ||
[[Category: aldolase]] | [[Category: aldolase]] | ||
[[Category: dehydratase]] | [[Category: dehydratase]] | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:30:28 2008'' |
Revision as of 21:30, 30 March 2008
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| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Porphobilinogen synthase, with EC number 4.2.1.24 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Mon Mar 31 00:30:28 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. | Aldolase | Dehydratase | Heme biosynthesis | Lyase | Tetrapyrrole synthesis | Tim barrel | Zinc
