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Magnesium in PDB 2cjm: Mechanism of Cdk Inhibition By Active Site Phosphorylation: CDK2 Y15P T160P in Complex with Cyclin A Structure

Enzymatic activity of Mechanism of Cdk Inhibition By Active Site Phosphorylation: CDK2 Y15P T160P in Complex with Cyclin A Structure

All present enzymatic activity of Mechanism of Cdk Inhibition By Active Site Phosphorylation: CDK2 Y15P T160P in Complex with Cyclin A Structure:
2.7.1.37;

Protein crystallography data

The structure of Mechanism of Cdk Inhibition By Active Site Phosphorylation: CDK2 Y15P T160P in Complex with Cyclin A Structure, PDB code: 2cjm was solved by J.P.I.Welburn, J.Tucker, T.Johnson, L.Lindert, L.Lindert, A.Willis, M.E.M.Noble, J.A.Endicott, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 100.00 / 2.3
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 73.801, 133.202, 147.585, 90.00, 90.00, 90.00
R / Rfree (%) 20.1 / 26.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Mechanism of Cdk Inhibition By Active Site Phosphorylation: CDK2 Y15P T160P in Complex with Cyclin A Structure (pdb code 2cjm). 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 Mechanism of Cdk Inhibition By Active Site Phosphorylation: CDK2 Y15P T160P in Complex with Cyclin A Structure, PDB code: 2cjm:

Magnesium binding site 1 out of 1 in 2cjm

Go back to Magnesium Binding Sites List in 2cjm
Magnesium binding site 1 out of 1 in the Mechanism of Cdk Inhibition By Active Site Phosphorylation: CDK2 Y15P T160P in Complex with Cyclin A Structure


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Mechanism of Cdk Inhibition By Active Site Phosphorylation: CDK2 Y15P T160P in Complex with Cyclin A Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1295

b:68.0
occ:1.00
 O2B A:ATP1294 2.5 0.1 1.0
O5' A:ATP1294 2.6 91.3 1.0
C5' A:ATP1294 3.3 84.0 1.0
O A:GLU12 3.5 59.9 1.0
C4' A:ATP1294 3.6 79.1 1.0
O1A A:ATP1294 3.6 94.5 1.0
O3' A:ATP1294 3.7 79.1 1.0
PA A:ATP1294 3.7 95.1 1.0
O2G A:ATP1294 3.8 0.4 1.0
PB A:ATP1294 3.9 0.1 1.0
C3' A:ATP1294 4.1 77.8 1.0
O3A A:ATP1294 4.2 98.5 1.0
C A:GLU12 4.3 59.8 1.0
O A:HOH2174 4.6 58.4 1.0
N A:GLU12 4.8 58.5 1.0
NE2 A:GLN131 4.8 41.8 1.0
O3B A:ATP1294 4.8 0.1 1.0
CA A:GLY13 4.8 60.6 1.0
PG A:ATP1294 4.9 0.1 1.0
O4' A:ATP1294 4.9 74.3 1.0
O1B A:ATP1294 4.9 0.6 1.0
N A:GLY13 4.9 60.4 1.0

Reference:

J.P.I.Welburn, J.Tucker, T.Johnson, L.Lindert, M.Morgan, A.Willis, M.E.M.Noble, J.A.Endicott. How Tyrosine 15 Phosphorylation Inhibits the Activity of Cyclin-Dependent Kinase 2-Cyclin A. J.Biol.Chem. V. 282 3173 2007.
ISSN: ISSN 0021-9258
PubMed: 17095507
DOI: 10.1074/JBC.M609151200
Page generated: Mon Dec 14 07:19:15 2020

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