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Magnesium in PDB 7c97: Cryo-Em Structure of An Escherichia Coli Rnap-Promoter Open Complex (Rpo) with Sspa

Enzymatic activity of Cryo-Em Structure of An Escherichia Coli Rnap-Promoter Open Complex (Rpo) with Sspa

All present enzymatic activity of Cryo-Em Structure of An Escherichia Coli Rnap-Promoter Open Complex (Rpo) with Sspa:
2.5.1.18; 2.7.7.6;

Other elements in 7c97:

The structure of Cryo-Em Structure of An Escherichia Coli Rnap-Promoter Open Complex (Rpo) with Sspa 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 An Escherichia Coli Rnap-Promoter Open Complex (Rpo) with Sspa (pdb code 7c97). 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 An Escherichia Coli Rnap-Promoter Open Complex (Rpo) with Sspa, PDB code: 7c97:

Magnesium binding site 1 out of 1 in 7c97

Go back to Magnesium Binding Sites List in 7c97
Magnesium binding site 1 out of 1 in the Cryo-Em Structure of An Escherichia Coli Rnap-Promoter Open Complex (Rpo) with Sspa


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 An Escherichia Coli Rnap-Promoter Open Complex (Rpo) with Sspa within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg2001

b:22.8
occ:1.00
OD2 D:ASP464 2.0 13.5 1.0
OD1 D:ASP460 2.1 12.7 1.0
OD2 D:ASP460 2.2 12.7 1.0
OD1 D:ASP464 2.3 13.5 1.0
CG D:ASP460 2.3 12.7 1.0
CG D:ASP464 2.4 13.5 1.0
OD1 D:ASP462 3.3 11.5 1.0
CB D:ASP460 3.7 12.7 1.0
O D:ASP460 3.9 12.7 1.0
CB D:ASP464 3.9 13.5 1.0
N D:ASP460 4.1 12.7 1.0
CG D:ASP462 4.1 11.5 1.0
NH2 D:ARG425 4.2 18.8 1.0
CA D:ASP460 4.3 12.7 1.0
OD2 D:ASP462 4.3 11.5 1.0
C D:ASP460 4.4 12.7 1.0
N D:ASP464 4.8 13.5 1.0
CA D:ASP464 4.8 13.5 1.0
CZ D:ARG425 5.0 18.8 1.0

Reference:

L.Wei, F.Yu. Structural Basis For Transcription Inhibition By E. Coli Sspa Nucleic Acids Res. 2020.
ISSN: ESSN 1362-4962
Page generated: Wed Oct 2 13:53:50 2024

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