Magnesium in PDB 4j99: Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Gain-of-Function K659T Mutation.

All present enzymatic activity of Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Gain-of-Function K659T Mutation.:
2.7.10.1;

The structure of Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Gain-of-Function K659T Mutation., PDB code: 4j99 was solved by H.Chen, M.Mohammadi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.31 / 1.85
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	278.508, 78.395, 73.197, 90.00, 101.02, 90.00
R / Rfree (%)	20.6 / 24

The binding sites of Magnesium atom in the Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Gain-of-Function K659T Mutation. (pdb code 4j99). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Gain-of-Function K659T Mutation., PDB code: 4j99:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Gain-of-Function K659T 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 Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Gain-of-Function K659T Mutation. within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg803 b:65.3 occ:1.00 HOB2 C:ACP802 2.2 0.5 1.0 OD2 C:ASP644 2.5 48.2 0.4 OD2 C:ASP644 2.6 47.9 0.6 O2B C:ACP802 2.7 91.3 1.0 CB C:ASP644 2.7 38.9 0.6 CB C:ASP644 2.7 39.1 0.4 OD1 C:ASN631 2.7 38.7 1.0 CG C:ASP644 2.8 46.0 0.4 CG C:ASP644 2.9 46.2 0.6 O1A C:ACP802 3.2 76.5 1.0 H3B2 C:ACP802 3.4 66.8 1.0 PB C:ACP802 3.8 73.3 1.0 CG C:ASN631 3.8 32.5 1.0 OD1 C:ASP644 3.9 48.1 0.6 OD1 C:ASP644 3.9 47.8 0.4 CA C:ASP644 3.9 33.8 0.4 CA C:ASP644 3.9 32.9 0.6 C3B C:ACP802 4.0 55.6 1.0 O3A C:ACP802 4.1 0.3 1.0 PA C:ACP802 4.2 78.1 1.0 O C:HOH985 4.3 45.4 1.0 O C:ARG630 4.4 33.1 1.0 N C:ASP644 4.4 31.1 1.0 CA C:ASN631 4.4 23.8 1.0 CB C:ASN631 4.5 26.2 1.0 H2' C:ACP802 4.6 76.2 1.0 O2A C:ACP802 4.7 80.5 1.0 H3B1 C:ACP802 4.7 66.8 1.0 ND2 C:ASN631 4.7 30.0 1.0 H8 C:ACP802 4.8 55.4 1.0 O2G C:ACP802 4.9 74.2 1.0 C C:ALA643 5.0 29.7 1.0

Magnesium binding site 2 out of 3 in the Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Gain-of-Function K659T 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 Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Gain-of-Function K659T Mutation. within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg803 b:51.5 occ:1.00 OD1 D:ASN631 2.0 46.9 1.0 O1A D:ACP802 2.1 47.3 1.0 OD2 D:ASP644 2.2 40.0 1.0 O1B D:ACP802 2.2 49.1 1.0 CG D:ASN631 3.1 49.8 1.0 CG D:ASP644 3.3 39.1 1.0 PB D:ACP802 3.4 55.4 1.0 PA D:ACP802 3.4 49.0 1.0 ND2 D:ASN631 3.7 44.0 1.0 CB D:ASP644 3.7 31.0 1.0 O3A D:ACP802 3.8 68.5 1.0 O2B D:ACP802 3.9 47.9 1.0 H5'2 D:ACP802 4.0 70.9 1.0 O5' D:ACP802 4.3 58.8 1.0 O D:HOH945 4.3 55.8 1.0 OD1 D:ASP644 4.4 42.5 1.0 O D:HOH970 4.4 70.6 1.0 CB D:ASN631 4.4 44.4 1.0 O D:ARG630 4.5 40.1 1.0 HOB2 D:ACP802 4.5 57.4 1.0 HOG3 D:ACP802 4.5 77.4 1.0 O2A D:ACP802 4.5 46.3 1.0 C5' D:ACP802 4.6 59.1 1.0 CA D:ASN631 4.7 35.6 1.0 O D:HOH984 4.8 47.4 1.0 OD2 D:ASP626 4.8 34.6 1.0 C3B D:ACP802 4.9 97.0 1.0 C D:ARG630 4.9 42.0 1.0 HO3' D:ACP802 4.9 85.0 1.0 CG D:ARG630 5.0 63.5 1.0

Magnesium binding site 3 out of 3 in the Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Gain-of-Function K659T Mutation.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Gain-of-Function K659T Mutation. within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg804 b:46.5 occ:1.00 HOB2 D:ACP802 2.3 57.4 1.0 O2B D:ACP802 2.5 47.9 1.0 OD1 D:ASP644 2.6 42.5 1.0 NZ D:LYS517 3.1 43.1 1.0 OE1 D:GLU534 3.1 41.3 1.0 CG D:ASP644 3.6 39.1 1.0 CA D:GLY646 3.7 30.2 1.0 CD D:GLU534 3.7 35.9 1.0 OE2 D:GLU534 3.8 35.4 1.0 O D:HOH936 3.8 50.5 1.0 O1G D:ACP802 3.8 59.5 1.0 OD2 D:ASP644 3.8 40.0 1.0 N D:GLY646 3.9 26.9 1.0 O D:HOH932 4.0 38.7 1.0 PB D:ACP802 4.1 55.4 1.0 CE D:LYS517 4.1 41.9 1.0 O1B D:ACP802 4.8 49.1 1.0 C D:GLY646 4.8 34.5 1.0 CB D:ASP644 4.9 31.0 1.0 H3B2 D:ACP802 4.9 0.4 1.0 O3A D:ACP802 4.9 68.5 1.0 C3B D:ACP802 5.0 97.0 1.0

H.Chen, Z.Huang, K.Dutta, S.Blais, T.A.Neubert, X.Li, D.Cowburn, N.J.Traaseth, M.Mohammadi. Cracking the Molecular Origin of Intrinsic Tyrosine Kinase Activity Through Analysis of Pathogenic Gain-of-Function Mutations. Cell Rep V. 4 376 2013.
ISSN: ESSN 2211-1247
PubMed: 23871672
DOI: 10.1016/J.CELREP.2013.06.025