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Magnesium in PDB 4y52: Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation.

Enzymatic activity of Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation.

All present enzymatic activity of Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation.:
2.7.7.6;

Protein crystallography data

The structure of Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation., PDB code: 4y52 was solved by L.Wang, J.Chong, D.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.27 / 3.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 166.703, 221.644, 192.410, 90.00, 100.35, 90.00
R / Rfree (%) 20.1 / 23.2

Other elements in 4y52:

The structure of Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation. also contains other interesting chemical elements:

Zinc (Zn) 8 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation. (pdb code 4y52). 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 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation., PDB code: 4y52:

Magnesium binding site 1 out of 1 in 4y52

Go back to Magnesium Binding Sites List in 4y52
Magnesium binding site 1 out of 1 in the Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation.


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 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1803

b:78.4
occ:1.00
OD2 A:ASP485 2.3 0.2 1.0
O3' R:G9 2.4 65.2 1.0
OD1 A:ASP483 2.4 56.3 1.0
OD1 A:ASP485 2.5 0.3 1.0
CB A:ASP481 2.6 82.0 1.0
CG A:ASP485 2.7 0.9 1.0
CG A:ASP483 3.1 73.8 1.0
CA A:ASP481 3.4 70.1 1.0
OD2 A:ASP483 3.5 83.8 1.0
O A:ASP481 3.5 84.0 1.0
N A:ASP481 3.6 54.6 1.0
C A:ASP481 3.6 71.4 1.0
C3' R:G9 3.6 65.0 1.0
O2' R:G9 3.7 94.8 1.0
CG A:ASP481 3.8 0.4 1.0
C4' R:G9 3.9 75.1 1.0
OD2 A:ASP481 4.1 0.8 1.0
N A:ASP483 4.1 77.9 1.0
CB A:ASP483 4.2 61.4 1.0
CB A:ASP485 4.2 87.8 1.0
C2' R:G9 4.2 64.7 1.0
N A:PHE482 4.4 49.9 1.0
CA A:ASP483 4.6 53.7 1.0
C5' R:G9 4.8 81.1 1.0
N A:ASP485 4.8 67.6 1.0
C A:ALA480 4.8 72.4 1.0
OD1 A:ASP481 4.9 0.8 1.0
C A:ASP483 4.9 46.7 1.0

Reference:

L.Wang, Y.Zhou, L.Xu, R.Xiao, X.Lu, L.Chen, J.Chong, H.Li, C.He, X.D.Fu, D.Wang. Molecular Basis For 5-Carboxycytosine Recognition By Rna Polymerase II Elongation Complex. Nature V. 523 621 2015.
ISSN: ESSN 1476-4687
PubMed: 26123024
DOI: 10.1038/NATURE14482
Page generated: Tue Aug 20 16:24:51 2024

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