Magnesium in PDB 4krc: Crystal Structure of PHO85-PCL10-Atp-Gamma-S Complex

All present enzymatic activity of Crystal Structure of PHO85-PCL10-Atp-Gamma-S Complex:
2.7.11.22;

The structure of Crystal Structure of PHO85-PCL10-Atp-Gamma-S Complex, PDB code: 4krc was solved by F.A.Quiocho, F.Zheng, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.44 / 2.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	50.145, 65.378, 80.254, 90.00, 100.61, 90.00
R / Rfree (%)	20.4 / 27

The binding sites of Magnesium atom in the Crystal Structure of PHO85-PCL10-Atp-Gamma-S Complex (pdb code 4krc). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of PHO85-PCL10-Atp-Gamma-S Complex, PDB code: 4krc:

Magnesium binding site 1 out of 1 in the Crystal Structure of PHO85-PCL10-Atp-Gamma-S Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of PHO85-PCL10-Atp-Gamma-S Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:67.1 occ:1.00 OD1 A:ASN138 2.5 52.4 1.0 O2A A:AGS402 2.6 60.6 1.0 O2G A:AGS402 2.6 69.5 1.0 O3B A:AGS402 2.7 58.9 1.0 O3' A:AGS402 3.0 55.2 1.0 PG A:AGS402 3.2 94.2 1.0 OD2 A:ASP151 3.2 53.0 1.0 CG A:ASN138 3.6 47.0 1.0 C5' A:AGS402 3.7 51.3 1.0 C3' A:AGS402 3.7 55.7 1.0 CB A:GLN137 3.8 42.1 1.0 PA A:AGS402 3.9 54.5 1.0 O A:GLN137 3.9 51.4 1.0 S1G A:AGS402 4.0 96.2 1.0 C A:GLN137 4.1 47.5 1.0 O5' A:AGS402 4.1 58.1 1.0 PB A:AGS402 4.1 63.9 1.0 C4' A:AGS402 4.1 55.9 1.0 O3A A:AGS402 4.2 53.4 1.0 CG A:ASP151 4.3 50.5 1.0 ND2 A:ASN138 4.3 47.2 1.0 CE A:LYS135 4.4 49.9 1.0 N A:ASN138 4.4 46.8 1.0 O3G A:AGS402 4.6 80.0 1.0 CA A:ASN138 4.6 43.2 1.0 CA A:GLN137 4.6 46.8 1.0 CB A:ASN138 4.7 40.9 1.0 NZ A:LYS135 4.9 58.1 1.0 CG A:GLN137 4.9 45.8 1.0 CB A:ASP151 4.9 43.7 1.0 O1B A:AGS402 4.9 61.1 1.0

F.Zheng, F.A.Quiocho. New Structural Insights Into Phosphorylation-Free Mechanism For Full Cyclin-Dependent Kinase (Cdk)-Cyclin Activity and Substrate Recognition. J.Biol.Chem. V. 288 30682 2013.
ISSN: ISSN 0021-9258
PubMed: 24022486
DOI: 10.1074/JBC.M113.502773