1idc
From Proteopedia
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|PDB= 1idc |SIZE=350|CAPTION= <scene name='initialview01'>1idc</scene>, resolution 2.5Å | |PDB= 1idc |SIZE=350|CAPTION= <scene name='initialview01'>1idc</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OXS:2-OXALOSUCCINIC+ACID'>OXS</scene> |
- | |ACTIVITY= [http://en.wikipedia.org/wiki/Isocitrate_dehydrogenase_(NADP(+)) Isocitrate dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.42 1.1.1.42] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Isocitrate_dehydrogenase_(NADP(+)) Isocitrate dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.42 1.1.1.42] </span> |
|GENE= ICD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= ICD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1idc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1idc OCA], [http://www.ebi.ac.uk/pdbsum/1idc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1idc RCSB]</span> | ||
}} | }} | ||
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[[Category: Stoddard, B L.]] | [[Category: Stoddard, B L.]] | ||
[[Category: Sweet, R M.]] | [[Category: Sweet, R M.]] | ||
- | [[Category: MG]] | ||
- | [[Category: OXS]] | ||
[[Category: oxidoreductase (nad(a)-choh(d))]] | [[Category: oxidoreductase (nad(a)-choh(d))]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:18:12 2008'' |
Revision as of 18:18, 30 March 2008
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, resolution 2.5Å | |||||||
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Ligands: | , | ||||||
Gene: | ICD (Escherichia coli) | ||||||
Activity: | Isocitrate dehydrogenase (NADP(+)), with EC number 1.1.1.42 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
ISOCITRATE DEHYDROGENASE FROM E.COLI (MUTANT K230M), STEADY-STATE INTERMEDIATE COMPLEX DETERMINED BY LAUE CRYSTALLOGRAPHY
Overview
Site-directed mutagenesis and Laue diffraction data to 2.5 A resolution were used to solve the structures of two sequential intermediates formed during the catalytic actions of isocitrate dehydrogenase. Both intermediates are distinct from the enzyme-substrate and enzyme-product complexes. Mutation of key catalytic residues changed the rate determining steps so that protein and substrate intermediates within the overall reaction pathway could be visualized.
About this Structure
1IDC is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase., Bolduc JM, Dyer DH, Scott WG, Singer P, Sweet RM, Koshland DE Jr, Stoddard BL, Science. 1995 Jun 2;268(5215):1312-8. PMID:7761851
Page seeded by OCA on Sun Mar 30 21:18:12 2008