Magnesium in PDB 6m6a: Cryo-Em Structure of Thermus Thermophilus Mfd in Complex with Rna Polymerase

Enzymatic activity of Cryo-Em Structure of Thermus Thermophilus Mfd in Complex with Rna Polymerase

All present enzymatic activity of Cryo-Em Structure of Thermus Thermophilus Mfd in Complex with Rna Polymerase:
2.7.7.6;

Other elements in 6m6a:

The structure of Cryo-Em Structure of Thermus Thermophilus Mfd in Complex with Rna Polymerase also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cryo-Em Structure of Thermus Thermophilus Mfd in Complex with Rna Polymerase (pdb code 6m6a). 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 Cryo-Em Structure of Thermus Thermophilus Mfd in Complex with Rna Polymerase, PDB code: 6m6a:

Magnesium binding site 1 out of 1 in 6m6a

Go back to Magnesium Binding Sites List in 6m6a
Magnesium binding site 1 out of 1 in the Cryo-Em Structure of Thermus Thermophilus Mfd in Complex with Rna Polymerase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cryo-Em Structure of Thermus Thermophilus Mfd in Complex with Rna Polymerase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg2003

b:0.2
occ:1.00
OD1 D:ASP739 2.1 0.0 1.0
OD2 D:ASP741 2.1 0.7 1.0
OD2 D:ASP743 2.1 0.0 1.0
OD1 D:ASP741 2.1 0.7 1.0
CG D:ASP741 2.4 0.7 1.0
CG D:ASP739 2.6 0.0 1.0
OD2 D:ASP739 2.8 0.0 1.0
CG D:ASP743 2.9 0.0 1.0
OD1 D:ASP743 2.9 0.0 1.0
CB D:ASP741 3.9 0.7 1.0
O D:ASP739 3.9 0.0 1.0
CB D:ASP739 3.9 0.0 1.0
NH2 D:ARG704 4.0 0.7 1.0
N D:ASP739 4.1 0.0 1.0
C D:ASP739 4.3 0.0 1.0
CB D:ASP743 4.3 0.0 1.0
CA D:ASP739 4.3 0.0 1.0
N D:ASP741 4.6 0.7 1.0
CA D:ASP741 4.7 0.7 1.0
C D:ASP741 5.0 0.7 1.0

Reference:

J.Shi, A.Wen, M.Zhao, S.Jin, L.You, Y.Shi, S.Dong, X.Hua, Y.Zhang, Y.Feng. Structural Basis of Mfd-Dependent Transcription Termination. Nucleic Acids Res. 2020.
ISSN: ESSN 1362-4962
Page generated: Mon Jan 25 09:25:25 2021

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