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Magnesium in PDB 2j0l: Crystal Structure of A the Active Conformation of the Kinase Domain of Focal Adhesion Kinase with A Phosphorylated Activation Loop.

Enzymatic activity of Crystal Structure of A the Active Conformation of the Kinase Domain of Focal Adhesion Kinase with A Phosphorylated Activation Loop.

All present enzymatic activity of Crystal Structure of A the Active Conformation of the Kinase Domain of Focal Adhesion Kinase with A Phosphorylated Activation Loop.:
2.7.10.2;

Protein crystallography data

The structure of Crystal Structure of A the Active Conformation of the Kinase Domain of Focal Adhesion Kinase with A Phosphorylated Activation Loop., PDB code: 2j0l was solved by D.Lietha, X.Cai, Y.Li, M.D.Schaller, M.J.Eck, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.48 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 44.312, 71.809, 86.939, 90.00, 90.00, 90.00
R / Rfree (%) 21.4 / 26.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of A the Active Conformation of the Kinase Domain of Focal Adhesion Kinase with A Phosphorylated Activation Loop. (pdb code 2j0l). 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 Crystal Structure of A the Active Conformation of the Kinase Domain of Focal Adhesion Kinase with A Phosphorylated Activation Loop., PDB code: 2j0l:

Magnesium binding site 1 out of 1 in 2j0l

Go back to Magnesium Binding Sites List in 2j0l
Magnesium binding site 1 out of 1 in the Crystal Structure of A the Active Conformation of the Kinase Domain of Focal Adhesion Kinase with A Phosphorylated Activation Loop.


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 A the Active Conformation of the Kinase Domain of Focal Adhesion Kinase with A Phosphorylated Activation Loop. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1688

b:37.3
occ:1.00
 O2G A:ANP1689 1.8 33.0 1.0
O A:HOH2094 1.9 29.4 1.0
O A:HOH2046 2.2 36.4 1.0
OD1 A:ASP564 2.3 34.9 1.0
O1B A:ANP1689 2.3 32.3 1.0
OD2 A:ASP564 2.6 36.6 1.0
CG A:ASP564 2.8 37.3 1.0
O A:HOH2010 3.3 65.1 1.0
PG A:ANP1689 3.3 34.0 1.0
PB A:ANP1689 3.7 32.7 1.0
NE2 A:GLN432 3.8 40.6 0.5
O A:HOH2090 3.9 42.4 1.0
OD1 A:ASP546 3.9 38.5 1.0
N3B A:ANP1689 3.9 32.4 1.0
O A:HOH2095 4.0 39.6 1.0
O1G A:ANP1689 4.0 34.0 1.0
O A:HOH2049 4.0 39.4 1.0
CB A:ASP564 4.3 37.3 1.0
O3G A:ANP1689 4.3 35.2 1.0
O2B A:ANP1689 4.4 33.6 1.0
CD A:GLN432 4.5 39.7 0.5
O A:HOH2045 4.5 38.1 1.0
CA A:GLY566 4.6 47.8 1.0
N A:GLY566 4.6 45.2 1.0
O1A A:ANP1689 4.8 34.8 1.0
O3A A:ANP1689 4.8 34.6 1.0
CG A:LEU567 4.9 52.7 1.0
N A:LEU567 4.9 51.0 1.0
OE1 A:GLN432 5.0 40.4 0.5

Reference:

D.Lietha, X.Cai, D.F.J.Ceccarelli, Y.Li, M.D.Schaller, M.J.Eck. Structural Basis For the Autoinhibition of Focal Adhesion Kinase Cell(Cambridge,Mass.) V. 129 1177 2007.
ISSN: ISSN 0092-8674
PubMed: 17574028
DOI: 10.1016/J.CELL.2007.05.041
Page generated: Wed Aug 14 00:21:35 2024

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