Magnesium in PDB 3q4z: Structure of Unphosphorylated PAK1 Kinase Domain

All present enzymatic activity of Structure of Unphosphorylated PAK1 Kinase Domain:
2.7.11.1;

The structure of Structure of Unphosphorylated PAK1 Kinase Domain, PDB code: 3q4z was solved by J.Wang, J.-W.Wu, Z.-X.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.99 / 1.89
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	62.988, 79.996, 65.664, 90.00, 107.51, 90.00
R / Rfree (%)	18.4 / 23.1

The binding sites of Magnesium atom in the Structure of Unphosphorylated PAK1 Kinase Domain (pdb code 3q4z). 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 Structure of Unphosphorylated PAK1 Kinase Domain, PDB code: 3q4z:

Magnesium binding site 1 out of 1 in the Structure of Unphosphorylated PAK1 Kinase Domain


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Unphosphorylated PAK1 Kinase Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1 b:69.9 occ:1.00 O A:HOH561 2.5 68.9 1.0 O1B A:ANP800 2.6 89.3 1.0 OD1 A:ASN394 2.6 28.3 1.0 O A:HOH558 3.2 63.6 1.0 O A:HOH556 3.2 62.2 1.0 O2G A:ANP800 3.3 93.2 1.0 CG A:ASN394 3.5 27.3 1.0 OD2 A:ASP407 3.9 38.1 1.0 ND2 A:ASN394 3.9 25.6 1.0 O3G A:ANP800 4.1 92.5 1.0 CE A:LYS391 4.1 29.1 1.0 PB A:ANP800 4.1 0.0 1.0 O A:HOH560 4.2 46.5 1.0 CB A:ASP393 4.2 31.1 1.0 PG A:ANP800 4.3 84.3 1.0 O A:ASP393 4.3 29.7 1.0 CG A:ASP407 4.4 40.4 1.0 O2B A:ANP800 4.5 0.0 1.0 NZ A:LYS391 4.5 28.1 1.0 C A:ASP393 4.5 27.6 1.0 O3A A:ANP800 4.6 99.0 1.0 CB A:ASP407 4.7 36.2 1.0 CB A:ASN394 4.8 30.0 1.0 N A:ASN394 4.8 26.3 1.0 O A:HOH89 4.8 47.0 1.0 N3B A:ANP800 4.9 85.3 1.0 CA A:ASN394 4.9 29.7 1.0 OG1 B:THR423 5.0 42.7 1.0

J.Wang, J.-W.Wu, Z.-X.Wang. Structural Insights Into the Autoactivation Mechanism of P21-Activated Protein Kinase Structure V. 19 1752 2011.
ISSN: ISSN 0969-2126
PubMed: 22153498
DOI: 10.1016/J.STR.2011.10.013