Magnesium in PDB 1rdq: Hydrolysis of Atp in the Crystal of Y204A Mutant of Camp-Dependent Protein Kinase

All present enzymatic activity of Hydrolysis of Atp in the Crystal of Y204A Mutant of Camp-Dependent Protein Kinase:
2.7.1.37;

The structure of Hydrolysis of Atp in the Crystal of Y204A Mutant of Camp-Dependent Protein Kinase, PDB code: 1rdq was solved by J.Yang, L.F.Ten Eyck, N.H.Xuong, S.S.Taylor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.26
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	57.760, 79.513, 97.739, 90.00, 90.00, 90.00
R / Rfree (%)	13.2 / 16.2

The binding sites of Magnesium atom in the Hydrolysis of Atp in the Crystal of Y204A Mutant of Camp-Dependent Protein Kinase (pdb code 1rdq). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Hydrolysis of Atp in the Crystal of Y204A Mutant of Camp-Dependent Protein Kinase, PDB code: 1rdq:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Hydrolysis of Atp in the Crystal of Y204A Mutant of Camp-Dependent Protein Kinase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Hydrolysis of Atp in the Crystal of Y204A Mutant of Camp-Dependent Protein Kinase within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg601 b:6.5 occ:1.00 O4 E:PO4598 1.7 11.3 0.8 O2A E:ATP600 1.9 7.7 0.2 O2A E:ADP599 2.0 8.0 0.8 O E:HOH1146 2.0 10.0 1.0 OD2 E:ASP184 2.0 7.3 1.0 OD1 E:ASN171 2.1 9.2 1.0 O3B E:ADP599 2.1 12.0 0.8 O2G E:ATP600 2.1 5.8 0.2 O3B E:ATP600 2.3 7.5 0.2 PG E:ATP600 2.8 6.4 0.2 P E:PO4598 3.0 11.1 0.8 CG E:ASN171 3.0 8.2 1.0 CG E:ASP184 3.1 5.7 1.0 PA E:ATP600 3.2 8.1 0.2 PA E:ADP599 3.3 9.2 0.8 PB E:ADP599 3.4 10.0 0.8 ND2 E:ASN171 3.4 8.5 1.0 PB E:ATP600 3.4 8.2 0.2 CB E:ASP184 3.5 6.3 1.0 O2 E:PO4598 3.5 8.5 0.8 O3A E:ATP600 3.6 9.4 0.2 O3A E:ADP599 3.6 11.1 0.8 O3G E:ATP600 3.7 6.5 0.2 MG E:MG602 3.8 7.5 1.0 O1B E:ADP599 3.8 8.4 0.8 O1 E:PO4598 3.8 12.9 0.8 O1B E:ATP600 3.8 7.9 0.2 O1G E:ATP600 4.0 10.8 0.2 O1A E:ATP600 4.1 9.3 0.2 O I:HOH1100 4.1 31.8 1.0 OD1 E:ASP184 4.1 6.4 1.0 O3 E:PO4598 4.2 11.3 0.8 O1A E:ADP599 4.2 10.3 0.8 O5' E:ATP600 4.3 8.4 0.2 O3' E:ADP599 4.3 8.8 0.8 O5' E:ADP599 4.3 8.4 0.8 O3' E:ATP600 4.3 9.3 0.2 CB E:ASN171 4.4 6.9 1.0 C5' E:ATP600 4.4 7.8 0.2 C5' E:ADP599 4.4 7.9 0.8 CE E:LYS168 4.5 9.4 1.0 OD2 E:ASP166 4.6 10.2 1.0 O2B E:ADP599 4.6 11.6 0.8 O2B E:ATP600 4.7 11.0 0.2 C3' E:ADP599 4.8 7.6 0.8 O E:HOH1029 4.8 9.8 1.0 C3' E:ATP600 4.8 7.6 0.2 CA E:ASN171 4.8 6.5 1.0 NZ E:LYS168 4.9 12.1 1.0 O E:GLU170 4.9 8.2 1.0 CA E:ASP184 5.0 5.2 1.0 CA E:GLY52 5.0 16.9 1.0

Magnesium binding site 2 out of 2 in the Hydrolysis of Atp in the Crystal of Y204A Mutant of Camp-Dependent Protein Kinase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Hydrolysis of Atp in the Crystal of Y204A Mutant of Camp-Dependent Protein Kinase within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg602 b:7.5 occ:1.00 O2 E:PO4598 1.9 8.5 0.8 O1B E:ATP600 2.0 7.9 0.2 O3G E:ATP600 2.0 6.5 0.2 O E:HOH1028 2.1 9.7 1.0 O1B E:ADP599 2.1 8.4 0.8 O E:HOH1029 2.1 9.8 1.0 OD2 E:ASP184 2.2 7.3 1.0 OD1 E:ASP184 2.2 6.4 1.0 CG E:ASP184 2.5 5.7 1.0 PG E:ATP600 3.1 6.4 0.2 PB E:ATP600 3.1 8.2 0.2 P E:PO4598 3.2 11.1 0.8 PB E:ADP599 3.2 10.0 0.8 O3B E:ATP600 3.3 7.5 0.2 O3B E:ADP599 3.3 12.0 0.8 O2G E:ATP600 3.6 5.8 0.2 O4 E:PO4598 3.7 11.3 0.8 MG E:MG601 3.8 6.5 1.0 CD1 E:PHE54 3.9 11.4 1.0 OD2 E:ASP166 4.0 10.2 1.0 CB E:ASP184 4.1 6.3 1.0 O2B E:ATP600 4.1 11.0 0.2 O3 E:PO4598 4.2 11.3 0.8 O E:HOH1033 4.2 9.9 1.0 O2B E:ADP599 4.2 11.6 0.8 CE1 E:PHE54 4.2 10.6 1.0 CA E:GLY186 4.3 5.6 1.0 NZ E:LYS72 4.3 8.2 1.0 O3A E:ATP600 4.3 9.4 0.2 O3A E:ADP599 4.3 11.1 0.8 O1 E:PO4598 4.3 12.9 0.8 O1G E:ATP600 4.4 10.8 0.2 O2A E:ATP600 4.4 7.7 0.2 N E:GLY186 4.5 5.6 1.0 O2A E:ADP599 4.5 8.0 0.8 PA E:ATP600 4.7 8.1 0.2 PA E:ADP599 4.8 9.2 0.8 O1A E:ATP600 4.8 9.3 0.2 CA E:ASP184 4.9 5.2 1.0 O E:HOH1030 4.9 12.6 1.0 ND2 E:ASN171 5.0 8.5 1.0

J.Yang, L.F.Ten Eyck, N.H.Xuong, S.S.Taylor. Crystal Structure of A Camp-Dependent Protein Kinase Mutant at 1.26A: New Insights Into the Catalytic Mechanism. J.Mol.Biol. V. 336 473 2004.
ISSN: ISSN 0022-2836
PubMed: 14757059
DOI: 10.1016/J.JMB.2003.11.044