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Magnesium in PDB 1ta0: Three-Dimensional Structure of A Rna-Polymerase II Binding Protein with Associated Ligand.

Enzymatic activity of Three-Dimensional Structure of A Rna-Polymerase II Binding Protein with Associated Ligand.

All present enzymatic activity of Three-Dimensional Structure of A Rna-Polymerase II Binding Protein with Associated Ligand.:
3.1.3.16;

Protein crystallography data

The structure of Three-Dimensional Structure of A Rna-Polymerase II Binding Protein with Associated Ligand., PDB code: 1ta0 was solved by T.Kamenski, S.Heilmeier, T.Meinhart, P.Cramer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.10
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 117.820, 47.170, 40.070, 90.00, 90.00, 90.00
R / Rfree (%) 20.7 / 22.7

Other elements in 1ta0:

The structure of Three-Dimensional Structure of A Rna-Polymerase II Binding Protein with Associated Ligand. also contains other interesting chemical elements:

Fluorine (F) 3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Three-Dimensional Structure of A Rna-Polymerase II Binding Protein with Associated Ligand. (pdb code 1ta0). 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 Three-Dimensional Structure of A Rna-Polymerase II Binding Protein with Associated Ligand., PDB code: 1ta0:

Magnesium binding site 1 out of 1 in 1ta0

Go back to Magnesium Binding Sites List in 1ta0
Magnesium binding site 1 out of 1 in the Three-Dimensional Structure of A Rna-Polymerase II Binding Protein with Associated Ligand.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Three-Dimensional Structure of A Rna-Polymerase II Binding Protein with Associated Ligand. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg273

b:17.7
occ:1.00
 O A:ASP98 2.1 7.9 1.0
F2 A:BFD96 2.1 20.0 1.0
OD2 A:BFD96 2.3 13.6 1.0
OD1 A:ASN207 2.3 7.0 1.0
O A:HOH380 2.4 16.9 1.0
O A:HOH290 2.5 13.2 1.0
CG A:BFD96 3.2 11.9 1.0
C A:ASP98 3.3 9.5 1.0
CG A:ASN207 3.3 7.1 1.0
BE A:BFD96 3.4 20.0 1.0
OD1 A:BFD96 3.5 10.2 1.0
ND2 A:ASN207 3.7 8.9 1.0
CA A:ASP98 4.0 9.3 1.0
CB A:ASP98 4.1 9.8 1.0
OD1 A:ASP206 4.2 8.6 1.0
OG1 A:THR100 4.2 9.8 1.0
N A:ASP98 4.2 8.1 1.0
CB A:GLU99 4.3 10.8 1.0
O A:HOH381 4.3 11.6 1.0
F3 A:BFD96 4.3 20.0 1.0
OE1 A:GLU99 4.3 18.7 1.0
N A:GLU99 4.4 9.3 1.0
F1 A:BFD96 4.4 20.0 1.0
OG A:SER208 4.4 18.5 1.0
CB A:BFD96 4.6 8.9 1.0
CB A:ASN207 4.7 9.1 1.0
CA A:GLU99 4.7 9.1 1.0
N A:THR100 4.8 9.6 1.0
N A:ASN207 4.8 7.7 1.0
C A:GLU99 4.9 8.9 1.0
C A:LEU97 5.0 6.4 1.0

Reference:

T.Kamenski, S.Heilmeier, T.Meinhart, P.Cramer. Structure and Mechanism of Rna Polymerase II Ctd Phosphatases. Mol.Cell V. 15 399 2004.
ISSN: ISSN 1097-2765
PubMed: 15304220
DOI: 10.1016/J.MOLCEL.2004.06.035
Page generated: Mon Dec 14 06:51:02 2020

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