Magnesium in PDB 6n58: Cryo-Em Structure of Escherichia Coli Rnap Polymerase Bound with Trar in Conformation II

Enzymatic activity of Cryo-Em Structure of Escherichia Coli Rnap Polymerase Bound with Trar in Conformation II

All present enzymatic activity of Cryo-Em Structure of Escherichia Coli Rnap Polymerase Bound with Trar in Conformation II:
2.7.7.6;

Other elements in 6n58:

The structure of Cryo-Em Structure of Escherichia Coli Rnap Polymerase Bound with Trar in Conformation II also contains other interesting chemical elements:

Zinc (Zn) 3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cryo-Em Structure of Escherichia Coli Rnap Polymerase Bound with Trar in Conformation II (pdb code 6n58). 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 Escherichia Coli Rnap Polymerase Bound with Trar in Conformation II, PDB code: 6n58:

Magnesium binding site 1 out of 1 in 6n58

Go back to Magnesium Binding Sites List in 6n58
Magnesium binding site 1 out of 1 in the Cryo-Em Structure of Escherichia Coli Rnap Polymerase Bound with Trar in Conformation II


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 Escherichia Coli Rnap Polymerase Bound with Trar in Conformation II within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Mg1501

b:10.2
occ:1.00
OD2 J:ASP464 1.9 11.2 1.0
OD1 J:ASP464 2.2 11.2 1.0
CG J:ASP464 2.3 11.2 1.0
OD1 J:ASP460 3.1 14.6 1.0
OD1 J:ASP462 3.2 14.6 1.0
OD2 J:ASP460 3.7 14.6 1.0
CB J:ASP464 3.8 11.2 1.0
CG J:ASP460 3.8 14.6 1.0
NH2 J:ARG425 4.1 13.0 1.0
CG J:ASP462 4.2 14.6 1.0
OD2 J:ASP462 4.4 14.6 1.0
CA J:ASP464 4.6 11.2 1.0
N J:ASP464 4.7 11.2 1.0

Reference:

J.Chen, S.Gopalkrishnan, C.Chiu, A.Y.Chen, E.A.Campbell, R.L.Gourse, W.Ross, S.A.Darst. E. Colitrar Allosterically Regulates Transcription Initiation By Altering Rna Polymerase Conformation. Elife V. 8 2019.
ISSN: ESSN 2050-084X
PubMed: 31841111
DOI: 10.7554/ELIFE.49375
Page generated: Mon Dec 14 23:39:24 2020

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