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Magnesium in PDB 2b9f: Crystal Structure of Non-Phosphorylated FUS3

Enzymatic activity of Crystal Structure of Non-Phosphorylated FUS3

All present enzymatic activity of Crystal Structure of Non-Phosphorylated FUS3:
2.7.1.37;

Protein crystallography data

The structure of Crystal Structure of Non-Phosphorylated FUS3, PDB code: 2b9f was solved by A.Remenyi, M.C.Good, R.P.Bhattacharyya, W.A.Lim, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.700, 62.470, 87.168, 90.00, 90.00, 90.00
R / Rfree (%) 21.3 / 25.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Non-Phosphorylated FUS3 (pdb code 2b9f). 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 Non-Phosphorylated FUS3, PDB code: 2b9f:

Magnesium binding site 1 out of 1 in 2b9f

Go back to Magnesium Binding Sites List in 2b9f
Magnesium binding site 1 out of 1 in the Crystal Structure of Non-Phosphorylated FUS3


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 Non-Phosphorylated FUS3 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg600

b:14.6
occ:1.00
O3B A:ADP500 2.0 14.3 1.0
OD2 A:ASP155 2.0 13.8 1.0
O2A A:ADP500 2.0 13.9 1.0
OD1 A:ASN142 2.1 9.6 1.0
O A:HOH856 2.2 14.6 1.0
O A:HOH857 2.2 14.7 1.0
CG A:ASP155 3.0 12.5 1.0
CG A:ASN142 3.1 10.3 1.0
PB A:ADP500 3.2 15.9 1.0
PA A:ADP500 3.3 14.1 1.0
ND2 A:ASN142 3.5 12.2 1.0
O3A A:ADP500 3.5 15.7 1.0
O2B A:ADP500 3.8 17.8 1.0
CB A:ASP155 3.8 11.3 1.0
OD1 A:ASP155 3.8 13.0 1.0
O A:HOH786 4.1 25.3 1.0
O A:HOH728 4.2 26.2 1.0
O5' A:ADP500 4.2 16.1 1.0
C5' A:ADP500 4.3 15.5 1.0
O1A A:ADP500 4.4 14.8 1.0
O A:HOH775 4.4 34.1 1.0
CB A:ASN142 4.5 10.1 1.0
O1B A:ADP500 4.5 16.4 1.0
OG A:SER141 4.5 15.2 1.0
O A:HOH727 4.5 29.7 1.0
CA A:ASN142 4.8 10.7 1.0
O3' A:ADP500 4.8 14.1 1.0
O A:SER141 4.8 13.1 1.0
NH2 A:ARG55 4.8 12.8 1.0
OD2 A:ASP137 4.9 12.9 1.0

Reference:

A.Remenyi, M.C.Good, R.P.Bhattacharyya, W.A.Lim. The Role of Docking Interactions in Mediating Signaling Input, Output, and Discrimination in the Yeast Mapk Network. Mol.Cell V. 20 951 2005.
ISSN: ISSN 1097-2765
PubMed: 16364919
DOI: 10.1016/J.MOLCEL.2005.10.030
Page generated: Tue Aug 13 21:48:09 2024

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