1APM

2.0 ANGSTROM REFINED CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH A PEPTIDE INHIBITOR AND DETERGENT

Summary for 1APM

• Entry DOI: 10.2210/pdb1apm/pdb
• Descriptor: cAMP-DEPENDENT PROTEIN KINASE, PEPTIDE INHIBITOR PKI(5-24), N-OCTANE, ... (4 entities in total)
• Functional Keywords: transferase(phosphotransferase)
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 2
• Total formula weight: 43061.94

Authors

Knighton, D.R.,Bell, S.M.,Zheng, J.,Teneyck, L.F.,Xuong, N.-H.,Taylor, S.S.,Sowadski, J.M. (deposition date: 1993-01-18, release date: 1993-04-15, Last modification date: 2024-10-09)

Primary citation

Knighton, D.R.,Bell, S.M.,Zheng, J.,Ten Eyck, L.F.,Xuong, N.H.,Taylor, S.S.,Sowadski, J.M.
2.0 A refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with a peptide inhibitor and detergent.
Acta Crystallogr.,Sect.D, 49:357-361, 1993

PubMed Abstract: . A mutant (Serl39Ala) of the mouse recombinant catalytic (C) subunit of cAMP-dependent protein kinase was co-crystallized with a peptide inhibitor, PKI(5-24), and MEGA-8 (octanoyl-N-methylglucamide) detergent. This structure was refined using all observed data (30 248 reflections) between 30 and 1.95 A resolution to an R factor of 0.186. R.m.s. deviations of bond lengths and bond angles are 0.013 A and 2.3 degrees, respectively. The final model has 3075 atoms (207 solvent) with a mean B factor of 31.9 A(2). The placement of invariant protein-kinase residues and most C:PKI(5-24) interactions were confirmed, but register errors affecting residues 55-64 and 309-339 were corrected during refinement by shifting the affected sequences toward the C terminus along the previously determined backbone path. New details of C:PKI(5-24) interactions and the Ser338 autophosphorylation site are described, and the acyl group binding site near the catalytic subunit NH(2) terminus is identified.

PubMed: 15299526
DOI: 10.1107/S0907444993000502

Experimental method

X-RAY DIFFRACTION (2 Å)