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Magnesium in PDB 5ugx: Crystal Structure of the Tyrosine Kinase Domain of Fgf Receptor 2 Harboring A E565A/D650V Double Gain-of-Function Mutation

Enzymatic activity of Crystal Structure of the Tyrosine Kinase Domain of Fgf Receptor 2 Harboring A E565A/D650V Double Gain-of-Function Mutation

All present enzymatic activity of Crystal Structure of the Tyrosine Kinase Domain of Fgf Receptor 2 Harboring A E565A/D650V 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 E565A/D650V Double Gain-of-Function Mutation, PDB code: 5ugx 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) 38.18 / 2.35
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 66.973, 77.860, 115.809, 90.00, 90.00, 90.00
R / Rfree (%) 21.5 / 27.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Tyrosine Kinase Domain of Fgf Receptor 2 Harboring A E565A/D650V Double Gain-of-Function Mutation (pdb code 5ugx). 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 E565A/D650V Double Gain-of-Function Mutation, PDB code: 5ugx:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 5ugx

Go back to Magnesium Binding Sites List in 5ugx
Magnesium binding site 1 out of 2 in the Crystal Structure of the Tyrosine Kinase Domain of Fgf Receptor 2 Harboring A E565A/D650V 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 E565A/D650V Double Gain-of-Function Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg804

b:48.8
occ:1.00
OD1 B:ASN631 2.4 26.2 1.0
O1B B:ACP803 2.5 51.0 1.0
OD2 B:ASP644 2.6 32.5 1.0
O1A B:ACP803 3.1 49.1 1.0
CG B:ASN631 3.3 25.7 1.0
ND2 B:ASN631 3.4 26.8 1.0
CG B:ASP644 3.8 31.2 1.0
PB B:ACP803 3.9 52.1 1.0
O B:HOH904 3.9 21.6 1.0
CD B:ARG630 4.2 27.9 1.0
OD2 B:ASP626 4.2 25.2 1.0
CG B:ARG630 4.2 27.8 1.0
O2B B:ACP803 4.3 52.4 1.0
NE B:ARG630 4.3 28.4 1.0
CB B:ASP644 4.4 27.3 1.0
PA B:ACP803 4.4 49.4 1.0
O3A B:ACP803 4.6 50.9 1.0
CB B:ASN631 4.7 23.4 1.0
OD1 B:ASP644 4.7 31.7 1.0
O B:ARG630 5.0 25.2 1.0

Magnesium binding site 2 out of 2 in 5ugx

Go back to Magnesium Binding Sites List in 5ugx
Magnesium binding site 2 out of 2 in the Crystal Structure of the Tyrosine Kinase Domain of Fgf Receptor 2 Harboring A E565A/D650V 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 E565A/D650V Double Gain-of-Function Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg804

b:40.7
occ:1.00
OD1 A:ASN631 2.1 46.2 1.0
O2B A:ACP803 2.2 47.0 1.0
OD2 A:ASP644 2.5 20.2 0.6
CG A:ASN631 2.9 37.6 1.0
ND2 A:ASN631 3.0 36.2 1.0
PB A:ACP803 3.6 53.2 1.0
CG A:ASP644 3.6 22.8 0.6
CG A:ASP644 3.7 20.6 0.4
OD1 A:ASP644 3.7 20.7 0.4
O A:HOH904 3.9 41.2 1.0
OD1 A:ASP626 3.9 21.3 1.0
OD2 A:ASP644 4.0 21.3 0.4
O2A A:ACP803 4.0 54.8 1.0
O1B A:ACP803 4.1 52.9 1.0
CB A:ASP644 4.2 21.3 0.6
CB A:ASP644 4.2 19.6 0.4
CD A:ARG630 4.3 29.0 1.0
C3B A:ACP803 4.3 55.8 1.0
CG A:ARG630 4.3 27.0 1.0
CB A:ASN631 4.4 31.7 1.0
NE A:ARG630 4.6 29.0 1.0
OD1 A:ASP644 4.7 20.6 0.6
O3A A:ACP803 4.8 54.0 1.0
CG A:ASP626 4.9 20.6 1.0
CA A:ASN631 5.0 26.1 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 Sep 30 05:18:55 2024

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