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Magnesium in PDB 4j96: Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic Gain-of-Function K659M Mutation Identified in Cervical Cancer.

Enzymatic activity of Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic Gain-of-Function K659M Mutation Identified in Cervical Cancer.

All present enzymatic activity of Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic Gain-of-Function K659M Mutation Identified in Cervical Cancer.:
2.7.10.1;

Protein crystallography data

The structure of Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic Gain-of-Function K659M Mutation Identified in Cervical Cancer., PDB code: 4j96 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) 47.55 / 2.30
Space group P 43 2 2
Cell size a, b, c (Å), α, β, γ (°) 73.852, 73.852, 310.716, 90.00, 90.00, 90.00
R / Rfree (%) 17.6 / 21.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic Gain-of-Function K659M Mutation Identified in Cervical Cancer. (pdb code 4j96). 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 Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic Gain-of-Function K659M Mutation Identified in Cervical Cancer., PDB code: 4j96:

Magnesium binding site 1 out of 1 in 4j96

Go back to Magnesium Binding Sites List in 4j96
Magnesium binding site 1 out of 1 in the Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic Gain-of-Function K659M Mutation Identified in Cervical Cancer.


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 Pathogenic Gain-of-Function K659M Mutation Identified in Cervical Cancer. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg805

b:60.0
occ:1.00
 O1A B:ACP803 2.1 0.1 1.0
H8 B:ACP803 3.1 35.7 1.0
H3B1 B:ACP803 3.2 0.3 1.0
NZ B:LYS517 3.2 58.1 1.0
PA B:ACP803 3.2 0.9 1.0
O5' B:ACP803 3.2 65.4 1.0
H2' B:ACP803 3.6 57.0 1.0
OD2 B:ASP644 3.7 49.4 1.0
O1G B:ACP803 3.7 0.5 1.0
CG B:ASP644 4.0 48.7 1.0
C8 B:ACP803 4.1 29.8 1.0
C3B B:ACP803 4.1 96.9 1.0
O B:HOH988 4.1 37.3 1.0
CE B:LYS517 4.2 52.0 1.0
O2A B:ACP803 4.3 0.1 1.0
O3A B:ACP803 4.3 0.5 1.0
CB B:ASP644 4.4 36.7 1.0
PG B:ACP803 4.5 0.8 1.0
CG2 B:VAL495 4.5 28.4 1.0
C2' B:ACP803 4.5 47.5 1.0
H3' B:ACP803 4.6 63.1 1.0
C5' B:ACP803 4.6 57.7 1.0
OD1 B:ASP644 4.7 52.9 1.0
H3B2 B:ACP803 4.7 0.3 1.0
N7 B:ACP803 4.8 32.7 1.0
PB B:ACP803 4.9 0.3 1.0
OD1 B:ASN631 5.0 21.2 1.0

Reference:

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
Page generated: Mon Aug 11 14:37:04 2025

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