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Magnesium in PDB 7c17: The Cryo-Em Structure of E. Coli Cuer Transcription Activation Complex with Fully Duplex Promoter Dna

Enzymatic activity of The Cryo-Em Structure of E. Coli Cuer Transcription Activation Complex with Fully Duplex Promoter Dna

All present enzymatic activity of The Cryo-Em Structure of E. Coli Cuer Transcription Activation Complex with Fully Duplex Promoter Dna:
2.7.7.6;

Other elements in 7c17:

The structure of The Cryo-Em Structure of E. Coli Cuer Transcription Activation Complex with Fully Duplex Promoter Dna also contains other interesting chemical elements:

Silver (Ag) 1 atom
Zinc (Zn) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The Cryo-Em Structure of E. Coli Cuer Transcription Activation Complex with Fully Duplex Promoter Dna (pdb code 7c17). 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 The Cryo-Em Structure of E. Coli Cuer Transcription Activation Complex with Fully Duplex Promoter Dna, PDB code: 7c17:

Magnesium binding site 1 out of 1 in 7c17

Go back to Magnesium Binding Sites List in 7c17
Magnesium binding site 1 out of 1 in the The Cryo-Em Structure of E. Coli Cuer Transcription Activation Complex with Fully Duplex Promoter Dna


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Cryo-Em Structure of E. Coli Cuer Transcription Activation Complex with Fully Duplex Promoter Dna within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg1503

b:35.5
occ:1.00
 OD1 D:ASP464 2.5 42.9 1.0
OD2 D:ASP464 3.1 42.9 1.0
CG D:ASP464 3.1 42.9 1.0
OD1 D:ASP460 4.0 40.9 1.0
OD2 D:ASP462 4.3 41.7 1.0
CB D:ASP462 4.3 41.7 1.0
CB D:ASP464 4.6 42.9 1.0
CG D:ASP462 4.7 41.7 1.0
O D:ASP460 4.8 40.9 1.0

Reference:

C.Fang, S.J.Philips, X.Wu, K.Chen, J.Shi, L.Shen, J.Xu, Y.Feng, T.V.O'halloran, Y.Zhang. Cuer Activates Transcription Through A Dna Distortion Mechanism. Nat.Chem.Biol. 2020.
ISSN: ESSN 1552-4469
PubMed: 32989300
DOI: 10.1038/S41589-020-00653-X
Page generated: Wed Oct 2 13:38:32 2024

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