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Magnesium in PDB 3qal: Crystal Structure of ARG280ALA Mutant of Catalytic Subunit of Camp- Dependent Protein Kinase

Enzymatic activity of Crystal Structure of ARG280ALA Mutant of Catalytic Subunit of Camp- Dependent Protein Kinase

All present enzymatic activity of Crystal Structure of ARG280ALA Mutant of Catalytic Subunit of Camp- Dependent Protein Kinase:
2.7.11.11;

Protein crystallography data

The structure of Crystal Structure of ARG280ALA Mutant of Catalytic Subunit of Camp- Dependent Protein Kinase, PDB code: 3qal was solved by J.Yang, J.Wu, J.Steichen, S.S.Taylor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 57.758, 80.082, 97.715, 90.00, 90.00, 90.00
R / Rfree (%) 17.6 / 19.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of ARG280ALA Mutant of Catalytic Subunit of Camp- Dependent Protein Kinase (pdb code 3qal). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of ARG280ALA Mutant of Catalytic Subunit of Camp- Dependent Protein Kinase, PDB code: 3qal:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3qal

Go back to Magnesium Binding Sites List in 3qal
Magnesium binding site 1 out of 2 in the Crystal Structure of ARG280ALA Mutant of Catalytic Subunit 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 Crystal Structure of ARG280ALA Mutant of Catalytic Subunit of Camp- Dependent Protein Kinase within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg352

b:6.5
occ:1.00
O2A E:ATP351 2.0 7.7 1.0
OD1 E:ASN171 2.0 7.2 1.0
O E:HOH620 2.1 6.8 1.0
OD2 E:ASP184 2.1 7.1 1.0
O2G E:ATP351 2.1 8.1 1.0
O3B E:ATP351 2.6 8.4 1.0
PG E:ATP351 2.9 8.8 1.0
CG E:ASN171 3.0 7.7 1.0
CG E:ASP184 3.1 8.6 1.0
PA E:ATP351 3.3 7.6 1.0
ND2 E:ASN171 3.4 6.4 1.0
CB E:ASP184 3.6 7.1 1.0
PB E:ATP351 3.6 9.8 1.0
O3G E:ATP351 3.7 6.2 1.0
O3A E:ATP351 3.8 8.1 1.0
MG E:MG353 3.9 8.7 1.0
O1B E:ATP351 3.9 8.8 1.0
CE E:LYS168 4.0 8.9 1.0
O1A E:ATP351 4.1 7.2 1.0
O1G E:ATP351 4.1 8.1 1.0
OD1 E:ASP184 4.2 6.8 1.0
NZ E:LYS168 4.2 10.3 1.0
O3' E:ATP351 4.3 7.7 1.0
OD1 E:ASP166 4.4 11.1 1.0
CB E:ASN171 4.4 6.9 1.0
O5' E:ATP351 4.4 7.5 1.0
O I:HOH755 4.6 12.9 1.0
C5' E:ATP351 4.7 6.8 1.0
O E:HOH818 4.7 10.5 1.0
CA E:ASN171 4.8 6.8 1.0
C3' E:ATP351 4.8 7.6 1.0
O E:GLU170 4.8 7.2 1.0
O2B E:ATP351 5.0 9.0 1.0

Magnesium binding site 2 out of 2 in 3qal

Go back to Magnesium Binding Sites List in 3qal
Magnesium binding site 2 out of 2 in the Crystal Structure of ARG280ALA Mutant of Catalytic Subunit 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 Crystal Structure of ARG280ALA Mutant of Catalytic Subunit of Camp- Dependent Protein Kinase within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg353

b:8.7
occ:1.00
O3G E:ATP351 2.0 6.2 1.0
O E:HOH608 2.0 6.1 1.0
O1B E:ATP351 2.1 8.8 1.0
O E:HOH818 2.1 10.5 1.0
OD1 E:ASP184 2.2 6.8 1.0
OD2 E:ASP184 2.2 7.1 1.0
CG E:ASP184 2.5 8.6 1.0
PG E:ATP351 3.1 8.8 1.0
PB E:ATP351 3.2 9.8 1.0
O3B E:ATP351 3.4 8.4 1.0
O2G E:ATP351 3.6 8.1 1.0
MG E:MG352 3.9 6.5 1.0
OD1 E:ASP166 4.0 11.1 1.0
CD2 E:PHE54 4.0 8.1 1.0
CB E:ASP184 4.0 7.1 1.0
O2B E:ATP351 4.1 9.0 1.0
O E:HOH607 4.3 9.9 1.0
CA E:GLY186 4.3 6.3 1.0
CE2 E:PHE54 4.3 8.7 1.0
NZ E:LYS72 4.3 8.6 1.0
O1G E:ATP351 4.4 8.1 1.0
O3A E:ATP351 4.4 8.1 1.0
O2A E:ATP351 4.4 7.7 1.0
N E:GLY186 4.5 8.4 1.0
O1A E:ATP351 4.5 7.2 1.0
PA E:ATP351 4.6 7.6 1.0
CB I:ALA21 4.8 10.3 1.0
CA E:ASP184 4.8 8.1 1.0
O E:HOH609 4.9 10.9 1.0
O E:ASP184 5.0 9.4 1.0
ND2 E:ASN171 5.0 6.4 1.0
C E:ASP184 5.0 8.9 1.0

Reference:

J.Yang, J.Wu, J.M.Steichen, A.P.Kornev, M.S.Deal, S.Li, B.Sankaran, V.L.Woods, S.S.Taylor. A Conserved Glu-Arg Salt Bridge Connects Coevolved Motifs That Define the Eukaryotic Protein Kinase Fold. J.Mol.Biol. V. 415 666 2012.
ISSN: ISSN 0022-2836
PubMed: 22138346
DOI: 10.1016/J.JMB.2011.11.035
Page generated: Thu Aug 15 10:00:49 2024

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