1idc

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|PDB= 1idc |SIZE=350|CAPTION= <scene name='initialview01'>1idc</scene>, resolution 2.5&Aring;
|PDB= 1idc |SIZE=350|CAPTION= <scene name='initialview01'>1idc</scene>, resolution 2.5&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=OXS:2-OXALOSUCCINIC ACID'>OXS</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OXS:2-OXALOSUCCINIC+ACID'>OXS</scene>
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|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]
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|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])
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|DOMAIN=
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|RELATEDENTRY=
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|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.]]
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[[Category: MG]]
 
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[[Category: OXS]]
 
[[Category: oxidoreductase (nad(a)-choh(d))]]
[[Category: oxidoreductase (nad(a)-choh(d))]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:48:55 2008''
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''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


PDB ID 1idc

Drag the structure with the mouse to rotate
, resolution 2.5Å
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

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