1atp: Difference between revisions

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[[Image:1atp.gif|left|200px]]
{{Seed}}
[[Image:1atp.png|left|200px]]


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{{STRUCTURE_1atp|  PDB=1atp  |  SCENE=  }}  
{{STRUCTURE_1atp|  PDB=1atp  |  SCENE=  }}  


'''2.2 ANGSTROM REFINED CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH MNATP AND A PEPTIDE INHIBITOR'''
===2.2 ANGSTROM REFINED CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH MNATP AND A PEPTIDE INHIBITOR===




==Overview==
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. The crystal structure of a ternary complex containing the catalytic subunit of cAMP-dependent protein kinase, ATP and a 20-residue inhibitor peptide was refined at a resolution of 2.2 A to an R value of 0.177. In order to identify the metal binding sites, the crystals, originally grown in the presence of low concentrations of Mg(2+), were soaked in Mn(2+). Two Mn(2+) ions were identified using an anomalous Fourier map. One Mn(2+) ion bridges the gamma- and beta-phosphates and interacts with Asp184 and two water molecules. The second Mn(2+) ion interacts with the side chains of Asn171 and Asp l84 as well as with a water molecule. Modeling a serine into the P site of the inhibitor peptide suggests a mechanism for phosphotransfer.
The line below this paragraph, {{ABSTRACT_PUBMED_15299527}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15299527 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15299527}}


==About this Structure==
==About this Structure==
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[[Category: Xuong, N H.]]
[[Category: Xuong, N H.]]
[[Category: Zheng, J.]]
[[Category: Zheng, J.]]
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