Magnesium in PDB 3q53: Structure of Phosphorylated PAK1 Kinase Domain in Complex with Atp

All present enzymatic activity of Structure of Phosphorylated PAK1 Kinase Domain in Complex with Atp:
2.7.11.1;

The structure of Structure of Phosphorylated PAK1 Kinase Domain in Complex with Atp, PDB code: 3q53 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)	29.95 / 2.09
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	48.982, 103.588, 121.967, 90.00, 90.00, 90.00
R / Rfree (%)	17.8 / 22.3

The binding sites of Magnesium atom in the Structure of Phosphorylated PAK1 Kinase Domain in Complex with Atp (pdb code 3q53). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of Phosphorylated PAK1 Kinase Domain in Complex with Atp, PDB code: 3q53:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of Phosphorylated PAK1 Kinase Domain in Complex with Atp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Phosphorylated PAK1 Kinase Domain in Complex with Atp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg554 b:76.0 occ:1.00 O A:HOH93 2.8 38.4 1.0 OD1 A:ASN394 2.9 27.5 1.0 O3B A:ATP1 3.0 0.5 1.0 MG A:MG555 3.1 64.9 1.0 O A:HOH97 3.1 39.4 1.0 O2B A:ATP1 3.4 83.3 1.0 O A:HOH84 3.6 42.5 1.0 OD2 A:ASP407 3.6 44.4 1.0 CG A:ASN394 3.8 30.3 1.0 PB A:ATP1 3.8 88.4 1.0 CE A:LYS391 3.8 24.6 1.0 ND2 A:ASN394 4.0 30.8 1.0 O1G A:ATP1 4.1 99.2 1.0 PG A:ATP1 4.1 97.8 1.0 O3A A:ATP1 4.2 0.5 1.0 NZ A:LYS391 4.2 24.6 1.0 O A:HOH80 4.4 41.9 1.0 CB A:ASP393 4.4 35.0 1.0 O3G A:ATP1 4.5 91.9 1.0 CG A:ASP407 4.6 40.1 1.0 CB A:ASP407 4.8 27.6 1.0 O A:ASP393 4.9 28.1 1.0 C A:ASP393 5.0 27.5 1.0

Magnesium binding site 2 out of 2 in the Structure of Phosphorylated PAK1 Kinase Domain in Complex with Atp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Phosphorylated PAK1 Kinase Domain in Complex with Atp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg555 b:64.9 occ:1.00 O A:HOH84 2.7 42.5 1.0 OD2 A:ASP407 2.9 44.4 1.0 O3A A:ATP1 3.0 0.5 1.0 MG A:MG554 3.1 76.0 1.0 CB A:ASP407 3.4 27.6 1.0 CG A:ASP407 3.4 40.1 1.0 OD1 A:ASN394 3.6 27.5 1.0 O3B A:ATP1 3.7 0.5 1.0 O1A A:ATP1 3.8 77.2 1.0 PB A:ATP1 3.9 88.4 1.0 O2B A:ATP1 3.9 83.3 1.0 PA A:ATP1 4.1 71.0 1.0 O A:HOH80 4.1 41.9 1.0 OD1 A:ASP407 4.5 39.6 1.0 O A:HOH97 4.5 39.4 1.0 CA A:ASP407 4.6 26.0 1.0 O A:HOH185 4.6 50.8 1.0 CG A:ASN394 4.7 30.3 1.0 NH2 A:ARG299 4.8 68.2 1.0 O5' A:ATP1 4.9 48.5 1.0 CG2 A:THR406 4.9 28.7 1.0 O3G A:ATP1 4.9 91.9 1.0 N A:ASP407 4.9 30.3 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