Manganese in PDB 1ql6: The Catalytic Mechanism of Phosphorylase Kinase Probed By Mutational Studies

All present enzymatic activity of The Catalytic Mechanism of Phosphorylase Kinase Probed By Mutational Studies:
2.7.1.38;

The structure of The Catalytic Mechanism of Phosphorylase Kinase Probed By Mutational Studies, PDB code: 1ql6 was solved by V.T.Skamnaki, D.J.Owen, M.E.M.Noble, E.D.Lowe, N.G.Oikonomakos, L.N.Johnson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	47.560, 68.171, 112.475, 90.00, 90.00, 90.00
R / Rfree (%)	24 / 33

The binding sites of Manganese atom in the The Catalytic Mechanism of Phosphorylase Kinase Probed By Mutational Studies (pdb code 1ql6). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the The Catalytic Mechanism of Phosphorylase Kinase Probed By Mutational Studies, PDB code: 1ql6:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the The Catalytic Mechanism of Phosphorylase Kinase Probed By Mutational Studies


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of The Catalytic Mechanism of Phosphorylase Kinase Probed By Mutational Studies within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn302 b:45.8 occ:1.00 OD1 A:ASP167 2.2 38.8 1.0 O3G A:ATP301 2.2 53.1 1.0 O2B A:ATP301 2.3 49.1 1.0 O A:HOH467 2.3 41.2 1.0 OD2 A:ASP167 2.4 41.8 1.0 CG A:ASP167 2.7 39.2 1.0 PG A:ATP301 3.3 55.8 1.0 PB A:ATP301 3.4 47.5 1.0 O3B A:ATP301 3.6 53.8 1.0 O2G A:ATP301 3.7 54.4 1.0 MN A:MN303 3.9 41.6 1.0 O A:HOH437 4.1 48.3 1.0 OD2 A:ASP149 4.2 40.5 1.0 CB A:ASP167 4.2 34.6 1.0 O1B A:ATP301 4.3 46.9 1.0 O2A A:ATP301 4.4 38.9 1.0 NZ A:LYS48 4.5 39.8 1.0 CA A:GLY169 4.5 40.4 1.0 O3A A:ATP301 4.5 43.1 1.0 O1G A:ATP301 4.5 56.5 1.0 N A:GLY169 4.6 38.9 1.0 O A:ASP167 4.9 40.9 1.0 PA A:ATP301 4.9 38.0 1.0 CE1 A:PHE170 4.9 40.5 1.0 CA A:ASP167 5.0 37.0 1.0

Manganese binding site 2 out of 2 in the The Catalytic Mechanism of Phosphorylase Kinase Probed By Mutational Studies


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of The Catalytic Mechanism of Phosphorylase Kinase Probed By Mutational Studies within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn303 b:41.6 occ:1.00 O2G A:ATP301 2.0 54.4 1.0 O2A A:ATP301 2.1 38.9 1.0 OD2 A:ASP167 2.2 41.8 1.0 OD1 A:ASN154 2.3 30.1 1.0 O A:HOH402 2.4 36.1 1.0 O3B A:ATP301 2.6 53.8 1.0 PG A:ATP301 2.8 55.8 1.0 CG A:ASP167 3.2 39.2 1.0 CG A:ASN154 3.3 31.2 1.0 PA A:ATP301 3.4 38.0 1.0 O3G A:ATP301 3.6 53.1 1.0 PB A:ATP301 3.7 47.5 1.0 CB A:ASP167 3.8 34.6 1.0 ND2 A:ASN154 3.8 33.0 1.0 O3A A:ATP301 3.8 43.1 1.0 MN A:MN302 3.9 45.8 1.0 O2B A:ATP301 4.0 49.1 1.0 O1G A:ATP301 4.1 56.5 1.0 OD1 A:ASP167 4.1 38.8 1.0 O3' A:ATP301 4.3 31.4 1.0 O5' A:ATP301 4.4 41.5 1.0 O A:HOH414 4.4 61.8 1.0 O1A A:ATP301 4.4 36.0 1.0 C5' A:ATP301 4.5 38.7 1.0 CB A:ASN154 4.6 31.5 1.0 O A:GLU153 4.8 40.1 1.0 OD2 A:ASP149 4.8 40.5 1.0 CE A:LYS151 4.9 47.8 1.0 O1B A:ATP301 4.9 46.9 1.0 CA A:ASN154 4.9 34.3 1.0

V.T.Skamnaki, D.J.Owen, M.E.Noble, E.D.Lowe, G.Lowe, N.G.Oikonomakos, L.N.Johnson. Catalytic Mechanism of Phosphorylase Kinase Probed By Mutational Studies. Biochemistry V. 38 14718 1999.
ISSN: ISSN 0006-2960
PubMed: 10545198
DOI: 10.1021/BI991454F