Manganese in PDB 3a62: Crystal Structure of Phosphorylated P70S6K1

All present enzymatic activity of Crystal Structure of Phosphorylated P70S6K1:
2.7.11.1;

The structure of Crystal Structure of Phosphorylated P70S6K1, PDB code: 3a62 was solved by T.Sunami, N.Byrne, R.E.Diehl, K.Funabashi, D.L.Hall, M.Ikuta, S.B.Patel, J.M.Shipman, R.F.Smith, I.Takahashi, J.Zugay-Murphy, Y.Iwasawa, K.J.Lumb, S.K.Munshi, S.Sharma, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.01 / 2.35
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	68.742, 68.742, 144.589, 90.00, 90.00, 90.00
R / Rfree (%)	23.6 / 27.7

The binding sites of Manganese atom in the Crystal Structure of Phosphorylated P70S6K1 (pdb code 3a62). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of Phosphorylated P70S6K1, PDB code: 3a62:

Manganese binding site 1 out of 1 in the Crystal Structure of Phosphorylated P70S6K1


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Phosphorylated P70S6K1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn38 b:47.8 occ:1.00 ND1 A:HIS251 2.0 50.9 1.0 SG A:CYS254 2.2 53.1 1.0 SG A:CYS240 2.3 59.3 1.0 CE1 A:HIS251 2.7 54.1 1.0 O A:HOH37 3.0 49.6 1.0 CB A:CYS254 3.1 55.8 1.0 CG A:HIS251 3.1 53.4 1.0 CB A:CYS240 3.4 61.0 1.0 CB A:HIS251 3.7 54.0 1.0 NE2 A:HIS251 3.9 55.2 1.0 CD2 A:HIS251 4.1 53.2 1.0 CA A:HIS251 4.3 58.0 1.0 O A:HIS251 4.3 59.1 1.0 CA A:CYS254 4.5 55.9 1.0 C A:HIS251 4.7 58.5 1.0 CA A:CYS240 4.8 62.3 1.0

T.Sunami, N.Byrne, R.E.Diehl, K.Funabashi, D.L.Hall, M.Ikuta, S.B.Patel, J.M.Shipman, R.F.Smith, I.Takahashi, J.Zugay-Murphy, Y.Iwasawa, K.J.Lumb, S.K.Munshi, S.Sharma. Structural Basis of Human P70 Ribosomal S6 Kinase-1 Regulation By Activation Loop Phosphorylation. J.Biol.Chem. V. 285 4587 2010.
ISSN: ISSN 0021-9258
PubMed: 19864428
DOI: 10.1074/JBC.M109.040667