1ATP

2.2 angstrom refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MNATP and a peptide inhibitor

Summary for 1ATP

• Entry DOI: 10.2210/pdb1atp/pdb
• Descriptor: cAMP-DEPENDENT PROTEIN KINASE, PEPTIDE INHIBITOR PKI(5-24), MANGANESE (II) ION, ... (5 entities in total)
• Functional Keywords: transferase(phosphotransferase)
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 2
• Total formula weight: 43500.78

Authors

Zheng, J.,Trafny, E.A.,Knighton, D.R.,Xuong, N.-H.,Taylor, S.S.,Teneyck, L.F.,Sowadski, J.M. (deposition date: 1993-01-08, release date: 1993-04-15, Last modification date: 2024-11-06)

Primary citation

Zheng, J.,Trafny, E.A.,Knighton, D.R.,Xuong, N.H.,Taylor, S.S.,Ten Eyck, L.F.,Sowadski, J.M.
2.2 A refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor.
Acta Crystallogr.,Sect.D, 49:362-365, 1993

PubMed Abstract: . 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.

PubMed: 15299527
DOI: 10.1107/S0907444993000423

Experimental method

X-RAY DIFFRACTION (2.2 Å)