1los: Difference between revisions
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|PDB= 1los |SIZE=350|CAPTION= <scene name='initialview01'>1los</scene>, resolution 1.90Å | |PDB= 1los |SIZE=350|CAPTION= <scene name='initialview01'>1los</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=UP6:6-AZA URIDINE 5'-MONOPHOSPHATE'>UP6</scene> | |LIGAND= <scene name='pdbligand=UP6:6-AZA+URIDINE+5'-MONOPHOSPHATE'>UP6</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Orotidine-5'-phosphate_decarboxylase Orotidine-5'-phosphate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.23 4.1.1.23] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Orotidine-5'-phosphate_decarboxylase Orotidine-5'-phosphate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.23 4.1.1.23] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1lol|1LOL]], [[1loq|1LOQ]], [[1lor|1LOR]], [[1lp6|1LP6]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1los FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1los OCA], [http://www.ebi.ac.uk/pdbsum/1los PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1los RCSB]</span> | |||
}} | }} | ||
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[[Category: Pai, E F.]] | [[Category: Pai, E F.]] | ||
[[Category: Wu, N.]] | [[Category: Wu, N.]] | ||
[[Category: tim barrel]] | [[Category: tim barrel]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:05:26 2008'' | ||
Revision as of 22:05, 30 March 2008
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| , resolution 1.90Å | |||||||
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| Ligands: | |||||||
| Activity: | Orotidine-5'-phosphate decarboxylase, with EC number 4.1.1.23 | ||||||
| Related: | 1LOL, 1LOQ, 1LOR, 1LP6
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
crystal structure of orotidine monophosphate decarboxylase mutant deltaR203A complexed with 6-azaUMP
OverviewOverview
The crystal structures of the enzyme orotidine-5'-monophosphate decarboxylase from Methanobacterium thermoautotrophicum complexed with its product UMP and the inhibitors 6-hydroxyuridine 5'-phosphate (BMP), XMP, and CMP are reported. A mutant version of the protein, in which four residues of the flexible phosphate-binding loop (180)Gly-Gly(190) were removed and Arg(203) was replaced by alanine, was also analyzed. The XMP and CMP complexes reveal a ligand-binding mode that is distinct from the one identified previously with the aromatic rings located outside the binding pocket. A potential pathway for ligand binding is discussed.
About this StructureAbout this Structure
1LOS is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of inhibitor complexes reveal an alternate binding mode in orotidine-5'-monophosphate decarboxylase., Wu N, Pai EF, J Biol Chem. 2002 Aug 2;277(31):28080-7. Epub 2002 May 13. PMID:12011084
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