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Magnesium in PDB 1i44: Crystallographic Studies of An Activation Loop Mutant of the Insulin Receptor Tyrosine Kinase

Enzymatic activity of Crystallographic Studies of An Activation Loop Mutant of the Insulin Receptor Tyrosine Kinase

All present enzymatic activity of Crystallographic Studies of An Activation Loop Mutant of the Insulin Receptor Tyrosine Kinase:
2.7.1.112;

Protein crystallography data

The structure of Crystallographic Studies of An Activation Loop Mutant of the Insulin Receptor Tyrosine Kinase, PDB code: 1i44 was solved by J.H.Till, A.J.Ablooglu, M.Frankel, R.A.Kohanski, S.R.Hubbard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 57.857, 69.578, 89.260, 90.00, 90.00, 90.00
R / Rfree (%) 21 / 26.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystallographic Studies of An Activation Loop Mutant of the Insulin Receptor Tyrosine Kinase (pdb code 1i44). 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 Crystallographic Studies of An Activation Loop Mutant of the Insulin Receptor Tyrosine Kinase, PDB code: 1i44:

Magnesium binding site 1 out of 1 in 1i44

Go back to Magnesium Binding Sites List in 1i44
Magnesium binding site 1 out of 1 in the Crystallographic Studies of An Activation Loop Mutant of the Insulin Receptor Tyrosine Kinase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystallographic Studies of An Activation Loop Mutant of the Insulin Receptor Tyrosine Kinase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg301

b:39.7
occ:1.00
 OD2 A:ASP1150 2.4 26.1 1.0
O A:HOH121 2.4 30.5 1.0
O1G A:ACP300 2.5 41.0 1.0
O A:HOH116 2.5 20.4 1.0
O2B A:ACP300 2.6 37.1 1.0
O A:HOH114 2.9 25.8 1.0
OD1 A:ASP1150 3.1 27.6 1.0
CG A:ASP1150 3.1 26.3 1.0
C3B A:ACP300 3.2 38.8 1.0
PG A:ACP300 3.4 41.7 1.0
PB A:ACP300 3.4 36.0 1.0
O A:HOH100 3.7 21.8 1.0
O A:HOH96 3.8 39.1 1.0
OD1 A:ASN1137 3.9 18.0 1.0
O2A A:ACP300 4.1 31.9 1.0
O2G A:ACP300 4.1 42.0 1.0
O A:HOH3 4.3 8.5 1.0
O3A A:ACP300 4.3 34.5 1.0
O A:HOH141 4.5 43.5 1.0
PA A:ACP300 4.5 33.0 1.0
CG A:ASN1137 4.5 15.1 1.0
O1A A:ACP300 4.5 30.2 1.0
CB A:ASP1150 4.6 24.4 1.0
O1B A:ACP300 4.6 35.5 1.0
O3G A:ACP300 4.7 42.5 1.0
O A:GLY1152 4.9 42.7 1.0

Reference:

J.H.Till, A.J.Ablooglu, M.Frankel, S.M.Bishop, R.A.Kohanski, S.R.Hubbard. Crystallographic and Solution Studies of An Activation Loop Mutant of the Insulin Receptor Tyrosine Kinase: Insights Into Kinase Mechanism. J.Biol.Chem. V. 276 10049 2001.
ISSN: ISSN 0021-9258
PubMed: 11124964
DOI: 10.1074/JBC.M010161200
Page generated: Mon Dec 14 06:02:12 2020

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