Potassium in PDB 1y8n: Crystal Structure of the PDK3-L2 Complex

All present enzymatic activity of Crystal Structure of the PDK3-L2 Complex:
2.3.1.12; 2.7.1.99;

The structure of Crystal Structure of the PDK3-L2 Complex, PDB code: 1y8n was solved by M.Kato, J.L.Chuang, R.M.Wynn, D.T.Chuang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.69 / 2.60
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	120.806, 120.806, 238.587, 90.00, 90.00, 120.00
R / Rfree (%)	21 / 24.8

The binding sites of Potassium atom in the Crystal Structure of the PDK3-L2 Complex (pdb code 1y8n). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Crystal Structure of the PDK3-L2 Complex, PDB code: 1y8n:

Potassium binding site 1 out of 1 in the Crystal Structure of the PDK3-L2 Complex


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of the PDK3-L2 Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:K501 b:71.7 occ:1.00 O A:SER20 2.5 51.5 1.0 O A:PHE372 2.5 51.1 1.0 O A:PHE22 2.6 56.2 1.0 OD1 A:ASN59 2.6 53.1 1.0 CG A:ASN59 3.5 55.2 1.0 C A:PHE22 3.5 56.0 1.0 C A:SER20 3.6 52.5 1.0 C A:PHE372 3.6 52.3 1.0 C A:ARG21 3.7 53.1 1.0 ND2 A:ASN59 3.7 52.3 1.0 O A:ARG21 3.8 51.2 1.0 CG1 A:VAL371 3.9 51.6 1.0 N A:PHE372 3.9 52.4 1.0 N A:PHE22 4.0 53.9 1.0 CA A:ARG21 4.0 53.6 1.0 CA A:PHE372 4.2 52.4 1.0 N A:ARG21 4.2 53.0 1.0 N A:SER23 4.3 56.2 1.0 CA A:SER23 4.3 56.5 1.0 CB A:PHE372 4.4 51.9 1.0 CA A:PHE22 4.4 54.9 1.0 C A:VAL371 4.7 53.9 1.0 CD A:PRO24 4.7 57.4 1.0 N A:ASN373 4.7 51.9 1.0 CA A:SER20 4.7 52.7 1.0 CD2 A:PHE372 4.8 52.7 1.0 CB A:ASN59 4.9 54.5 1.0 OG A:SER23 5.0 58.0 1.0 CA A:VAL371 5.0 53.9 1.0

M.Kato, J.L.Chuang, S.C.Tso, R.M.Wynn, D.T.Chuang. Crystal Structure of Pyruvate Dehydrogenase Kinase 3 Bound to Lipoyl Domain 2 of Human Pyruvate Dehydrogenase Complex. Embo J. V. 24 1763 2005.
ISSN: ISSN 0261-4189
PubMed: 15861126
DOI: 10.1038/SJ.EMBOJ.7600663