2c1h
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2c1h |SIZE=350|CAPTION= <scene name='initialview01'>2c1h</scene>, resolution 2.60Å | |PDB= 2c1h |SIZE=350|CAPTION= <scene name='initialview01'>2c1h</scene>, resolution 2.60Å | ||
|SITE= <scene name='pdbsite=AC1:Dsb+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Dsb+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=DSB:4,7-DIOXOSEBACIC+ACID'>DSB</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=2c1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c1h OCA], [http://www.ebi.ac.uk/pdbsum/2c1h PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2c1h RCSB]</span> | ||
}} | }} | ||
| Line 30: | Line 33: | ||
[[Category: Shoolingin-Jordan, P M.]] | [[Category: Shoolingin-Jordan, P M.]] | ||
[[Category: Wood, S P.]] | [[Category: Wood, S P.]] | ||
| - | [[Category: DSB]] | ||
| - | [[Category: MG]] | ||
[[Category: 5-aminolaevulinic acid dehydratase]] | [[Category: 5-aminolaevulinic acid dehydratase]] | ||
[[Category: alad]] | [[Category: alad]] | ||
| Line 39: | Line 40: | ||
[[Category: porphyrin biosynthesis]] | [[Category: porphyrin biosynthesis]] | ||
| - | ''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 02:14:59 2008'' |
Revision as of 23:14, 30 March 2008
| |||||||
| , resolution 2.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Porphobilinogen synthase, with EC number 4.2.1.24 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE X-RAY STRUCTURE OF CHLOROBIUM VIBRIOFORME 5-AMINOLAEVULINIC ACID DEHYDRATASE COMPLEXED WITH A DIACID INHIBITOR
Overview
The structure of Chlorobium vibrioforme 5-aminolaevulinic acid dehydratase (ALAD) complexed with the irreversible inhibitor 4,7-dioxosebacic acid has been solved. The inhibitor binds by forming Schiff-base linkages with lysines 200 and 253 at the active site. The structure reported here provides a definition of the interactions made by both of the substrate molecules (A-side and P-side substrates) with the C. vibrioforme ALAD and is compared and contrasted with structures of the same inhibitor bound to Escherichia coli and yeast ALAD. The structure suggests why 4,7-dioxosebacic acid is a better inhibitor of the zinc-dependent ALADs than of the zinc-independent ALADs.
About this Structure
2C1H is a Single protein structure of sequence from Prosthecochloris vibrioformis. Full crystallographic information is available from OCA.
Reference
Structure of Chlorobium vibrioforme 5-aminolaevulinic acid dehydratase complexed with a diacid inhibitor., Coates L, Beaven G, Erskine PT, Beale SI, Wood SP, Shoolingin-Jordan PM, Cooper JB, Acta Crystallogr D Biol Crystallogr. 2005 Dec;61(Pt 12):1594-8. Epub 2005, Nov 19. PMID:16304458
Page seeded by OCA on Mon Mar 31 02:14:59 2008
Categories: Porphobilinogen synthase | Prosthecochloris vibrioformis | Single protein | Beale, S. | Beaven, G. | Coates, L. | Cooper, J B. | Erskine, P T. | Shoolingin-Jordan, P M. | Wood, S P. | 5-aminolaevulinic acid dehydratase | Alad | Heme biosynthesis | Lyase | Magnesium | Porphyrin biosynthesis
