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Magnesium in PDB 6m6c: Cryoem Structure of Thermus Thermophilus Rna Polymerase Elongation Complex

Enzymatic activity of Cryoem Structure of Thermus Thermophilus Rna Polymerase Elongation Complex

All present enzymatic activity of Cryoem Structure of Thermus Thermophilus Rna Polymerase Elongation Complex:
2.7.7.6;

Other elements in 6m6c:

The structure of Cryoem Structure of Thermus Thermophilus Rna Polymerase Elongation Complex also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cryoem Structure of Thermus Thermophilus Rna Polymerase Elongation Complex (pdb code 6m6c). 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 Cryoem Structure of Thermus Thermophilus Rna Polymerase Elongation Complex, PDB code: 6m6c:

Magnesium binding site 1 out of 1 in 6m6c

Go back to Magnesium Binding Sites List in 6m6c
Magnesium binding site 1 out of 1 in the Cryoem Structure of Thermus Thermophilus Rna Polymerase Elongation Complex


Mono view


Stereo pair view

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

b:0.5
occ:1.00
OD1 D:ASP739 2.0 0.5 1.0
O3' R:A20 2.0 0.0 1.0
OD1 D:ASP741 2.1 0.6 1.0
OD2 D:ASP741 2.5 0.6 1.0
OD2 D:ASP739 2.6 0.5 1.0
CG D:ASP739 2.6 0.5 1.0
CG D:ASP741 2.6 0.6 1.0
OD1 D:ASP743 2.8 0.7 1.0
C3' R:A20 3.4 0.0 1.0
CG D:ASP743 3.6 0.7 1.0
OD2 D:ASP743 3.6 0.7 1.0
C4' R:A20 4.0 0.0 1.0
CB D:ASP739 4.0 0.5 1.0
CB D:ASP741 4.1 0.6 1.0
O2' R:A20 4.2 0.0 1.0
C2' R:A20 4.3 0.0 1.0
C5' R:A20 4.4 0.0 1.0
O D:ASP739 4.5 0.5 1.0
N D:ASP739 4.5 0.5 1.0
N D:ASP741 4.6 0.6 1.0
C D:ASP739 4.6 0.5 1.0
CA D:ASP739 4.6 0.5 1.0
CA D:ASP741 4.8 0.6 1.0
C D:ASP741 5.0 0.6 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: Tue Oct 1 11:34:40 2024

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