2cpk: Difference between revisions
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[[Image:2cpk.gif|left|200px]] | [[Image:2cpk.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CYCLIC ADENOSINE MONOPHOSPHATE-DEPENDENT PROTEIN KINASE''' | {{Structure | ||
|PDB= 2cpk |SIZE=350|CAPTION= <scene name='initialview01'>2cpk</scene>, resolution 2.7Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=PO3:PHOSPHITE ION'>PO3</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CYCLIC ADENOSINE MONOPHOSPHATE-DEPENDENT PROTEIN KINASE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2CPK is a [ | 2CPK is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry 1CPK. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CPK OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase., Knighton DR, Zheng JH, Ten Eyck LF, Ashford VA, Xuong NH, Taylor SS, Sowadski JM, Science. 1991 Jul 26;253(5018):407-14. PMID:[http:// | Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase., Knighton DR, Zheng JH, Ten Eyck LF, Ashford VA, Xuong NH, Taylor SS, Sowadski JM, Science. 1991 Jul 26;253(5018):407-14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1862342 1862342] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Non-specific serine/threonine protein kinase]] | [[Category: Non-specific serine/threonine protein kinase]] | ||
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[[Category: transferase(phosphotransferase)]] | [[Category: transferase(phosphotransferase)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:18:23 2008'' | ||
Revision as of 17:18, 20 March 2008
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| , resolution 2.7Å | |||||||
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| Ligands: | |||||||
| Activity: | Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CYCLIC ADENOSINE MONOPHOSPHATE-DEPENDENT PROTEIN KINASE
OverviewOverview
The crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase complexed with a 20-amino acid substrate analog inhibitor has been solved and partially refined at 2.7 A resolution to an R factor of 0.212. The magnesium adenosine triphosphate (MgATP) binding site was located by difference Fourier synthesis. The enzyme structure is bilobal with a deep cleft between the lobes. The cleft is filled by MgATP and a portion of the inhibitor peptide. The smaller lobe, consisting mostly of amino-terminal sequence, is associated with nucleotide binding, and its largely antiparallel beta sheet architecture constitutes an unusual nucleotide binding motif. The larger lobe is dominated by helical structure with a single beta sheet at the domain interface. This lobe is primarily involved in peptide binding and catalysis. Residues 40 through 280 constitute a conserved catalytic core that is shared by more than 100 protein kinases. Most of the invariant amino acids in this conserved catalytic core are clustered at the sites of nucleotide binding and catalysis.
About this StructureAbout this Structure
2CPK is a Protein complex structure of sequences from Mus musculus. This structure supersedes the now removed PDB entry 1CPK. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase., Knighton DR, Zheng JH, Ten Eyck LF, Ashford VA, Xuong NH, Taylor SS, Sowadski JM, Science. 1991 Jul 26;253(5018):407-14. PMID:1862342
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