Magnesium in PDB 5uhn: Crystal Structure of the Tyrosine Kinase Domain of Fgf Receptor 2 Harboring A N549H/E565A Double Gain-of-Function Mutation

Enzymatic activity of Crystal Structure of the Tyrosine Kinase Domain of Fgf Receptor 2 Harboring A N549H/E565A Double Gain-of-Function Mutation

All present enzymatic activity of Crystal Structure of the Tyrosine Kinase Domain of Fgf Receptor 2 Harboring A N549H/E565A Double Gain-of-Function Mutation:
2.7.10.1;

Protein crystallography data

The structure of Crystal Structure of the Tyrosine Kinase Domain of Fgf Receptor 2 Harboring A N549H/E565A Double Gain-of-Function Mutation, PDB code: 5uhn was solved by M.Mohammadi, H.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.28 / 2.91
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 67.334, 78.557, 116.546, 90.00, 90.00, 90.00
R / Rfree (%) 25.4 / 31.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Tyrosine Kinase Domain of Fgf Receptor 2 Harboring A N549H/E565A Double Gain-of-Function Mutation (pdb code 5uhn). 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 the Tyrosine Kinase Domain of Fgf Receptor 2 Harboring A N549H/E565A Double Gain-of-Function Mutation, PDB code: 5uhn:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 5uhn

Go back to Magnesium Binding Sites List in 5uhn
Magnesium binding site 1 out of 2 in the Crystal Structure of the Tyrosine Kinase Domain of Fgf Receptor 2 Harboring A N549H/E565A Double Gain-of-Function Mutation


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 the Tyrosine Kinase Domain of Fgf Receptor 2 Harboring A N549H/E565A Double Gain-of-Function Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg803

b:40.2
occ:1.00
OD1 A:ASN631 2.4 28.6 1.0
O2B A:ACP802 2.4 64.1 1.0
O2A A:ACP802 2.7 58.9 1.0
OD1 A:ASP644 3.0 26.5 1.0
OD2 A:ASP644 3.0 26.8 1.0
CG A:ASP644 3.2 25.9 1.0
O A:ARG630 3.5 32.4 1.0
PB A:ACP802 3.5 63.8 1.0
CG A:ASN631 3.6 28.4 1.0
O1B A:ACP802 3.7 63.6 1.0
PA A:ACP802 4.0 59.0 1.0
C A:ARG630 4.0 31.7 1.0
CA A:ASN631 4.1 28.2 1.0
O3A A:ACP802 4.2 61.6 1.0
CG A:ARG630 4.3 35.5 1.0
N A:ASN631 4.3 30.0 1.0
O3G A:ACP802 4.4 68.4 1.0
CB A:ASP644 4.4 24.1 1.0
CB A:ASN631 4.4 28.0 1.0
ND2 A:ASN631 4.5 28.5 1.0
O1A A:ACP802 4.7 59.3 1.0
CB A:ARG630 4.7 34.0 1.0
CD A:ARG630 4.8 37.4 1.0

Magnesium binding site 2 out of 2 in 5uhn

Go back to Magnesium Binding Sites List in 5uhn
Magnesium binding site 2 out of 2 in the Crystal Structure of the Tyrosine Kinase Domain of Fgf Receptor 2 Harboring A N549H/E565A Double Gain-of-Function Mutation


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 the Tyrosine Kinase Domain of Fgf Receptor 2 Harboring A N549H/E565A Double Gain-of-Function Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg803

b:80.8
occ:1.00
O B:ARG630 2.7 32.5 1.0
O1A B:ACP802 2.8 60.6 1.0
O1B B:ACP802 2.9 68.0 1.0
OD1 B:ASN631 3.1 29.1 1.0
OD1 B:ASP644 3.1 66.5 1.0
C B:ARG630 3.5 31.9 1.0
OD2 B:ASP644 3.6 67.0 1.0
CG B:ASP644 3.6 63.8 1.0
CA B:ASN631 3.9 28.9 1.0
PB B:ACP802 3.9 66.9 1.0
PA B:ACP802 4.0 61.0 1.0
O3A B:ACP802 4.0 64.3 1.0
O3' B:ACP802 4.0 54.6 1.0
N B:ASN631 4.1 30.6 1.0
CG B:ASN631 4.2 29.1 1.0
C3' B:ACP802 4.2 54.6 1.0
O2B B:ACP802 4.3 67.3 1.0
CG B:ARG630 4.4 35.2 1.0
CB B:ARG630 4.4 33.5 1.0
CA B:ARG630 4.6 32.4 1.0
CB B:ASN631 4.6 28.9 1.0
O5' B:ACP802 4.7 58.9 1.0
C5' B:ACP802 4.8 57.0 1.0
CB B:ASP644 5.0 56.2 1.0
C B:ASN631 5.0 29.4 1.0

Reference:

H.Chen, W.M.Marsiglia, M.K.Cho, Z.Huang, J.Deng, S.P.Blais, W.Gai, S.Bhattacharya, T.A.Neubert, N.J.Traaseth, M.Mohammadi. Elucidation of A Four-Site Allosteric Network in Fibroblast Growth Factor Receptor Tyrosine Kinases. Elife V. 6 2017.
ISSN: ESSN 2050-084X
PubMed: 28166054
DOI: 10.7554/ELIFE.21137
Page generated: Mon Dec 14 21:16:07 2020

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