Magnesium in PDB 8fiy: Cryo-Em Structure of E. Coli Rna Polymerase Elongation Complex in the Transcription-Translation Complex (Rnap in An Anti-Swiveled Conformation)

Enzymatic activity of Cryo-Em Structure of E. Coli Rna Polymerase Elongation Complex in the Transcription-Translation Complex (Rnap in An Anti-Swiveled Conformation)

All present enzymatic activity of Cryo-Em Structure of E. Coli Rna Polymerase Elongation Complex in the Transcription-Translation Complex (Rnap in An Anti-Swiveled Conformation):
2.7.7.6;

Other elements in 8fiy:

The structure of Cryo-Em Structure of E. Coli Rna Polymerase Elongation Complex in the Transcription-Translation Complex (Rnap in An Anti-Swiveled Conformation) 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 E. Coli Rna Polymerase Elongation Complex in the Transcription-Translation Complex (Rnap in An Anti-Swiveled Conformation) (pdb code 8fiy). 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 E. Coli Rna Polymerase Elongation Complex in the Transcription-Translation Complex (Rnap in An Anti-Swiveled Conformation), PDB code: 8fiy:

Magnesium binding site 1 out of 1 in 8fiy

Go back to Magnesium Binding Sites List in 8fiy
Magnesium binding site 1 out of 1 in the Cryo-Em Structure of E. Coli Rna Polymerase Elongation Complex in the Transcription-Translation Complex (Rnap in An Anti-Swiveled Conformation)


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 E. Coli Rna Polymerase Elongation Complex in the Transcription-Translation Complex (Rnap in An Anti-Swiveled Conformation) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg1503

b:487.6
occ:1.00
OD1 D:ASP464 2.4 461.9 1.0
O D:ASP462 2.7 505.9 1.0
O D:ASP460 2.7 550.0 1.0
N D:ASP462 3.3 505.9 1.0
C D:ASP462 3.3 505.9 1.0
CB D:ASP460 3.4 550.0 1.0
CG D:ASP464 3.5 461.9 1.0
CB D:ASP462 3.5 505.9 1.0
C D:ASP460 3.5 550.0 1.0
CA D:ASP462 3.5 505.9 1.0
O3' R:U9 3.5 457.2 1.0
O2' R:U9 3.5 457.2 1.0
C4' R:U9 3.7 457.2 1.0
CA D:ASP460 4.0 550.0 1.0
CG D:ASP460 4.0 550.0 1.0
OD2 D:ASP464 4.0 461.9 1.0
C3' R:U9 4.1 457.2 1.0
OD2 D:ASP460 4.2 550.0 1.0
N D:ASP464 4.3 461.9 1.0
N D:GLY463 4.4 490.6 1.0
C2' R:U9 4.4 457.2 1.0
C D:GLY463 4.4 490.6 1.0
C D:PHE461 4.4 460.2 1.0
N D:PHE461 4.5 460.2 1.0
N D:ASP460 4.5 550.0 1.0
CA D:ASP464 4.5 461.9 1.0
O D:GLY463 4.5 490.6 1.0
C5' R:U9 4.6 457.2 1.0
O4' R:U9 4.6 457.2 1.0
CB D:ASP464 4.6 461.9 1.0
NZ C:LYS1073 4.6 507.3 1.0
OD1 D:ASP460 4.7 550.0 1.0
CA D:PHE461 4.8 460.2 1.0
CG D:ASP462 4.9 505.9 1.0
CA D:GLY463 5.0 490.6 1.0

Reference:

L.M.Wee, A.B.Tong, A.J.Florez Ariza, C.Canari-Chumpitaz, P.Grob, E.Nogales, C.J.Bustamante. A Trailing Ribosome Speeds Up Rna Polymerase at the Expense of Transcript Fidelity Via Force and Allostery. Cell V. 186 1244 2023.
ISSN: ISSN 1097-4172
PubMed: 36931247
DOI: 10.1016/J.CELL.2023.02.008
Page generated: Tue Apr 11 16:08:21 2023

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