Magnesium in PDB 7khc: Escherichia Coli Rna Polymerase and RRNBP1 Promoter Closed Complex

Enzymatic activity of Escherichia Coli Rna Polymerase and RRNBP1 Promoter Closed Complex

All present enzymatic activity of Escherichia Coli Rna Polymerase and RRNBP1 Promoter Closed Complex:
2.7.7.6;

Other elements in 7khc:

The structure of Escherichia Coli Rna Polymerase and RRNBP1 Promoter Closed Complex also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Escherichia Coli Rna Polymerase and RRNBP1 Promoter Closed Complex (pdb code 7khc). 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 Escherichia Coli Rna Polymerase and RRNBP1 Promoter Closed Complex, PDB code: 7khc:

Magnesium binding site 1 out of 1 in 7khc

Go back to Magnesium Binding Sites List in 7khc
Magnesium binding site 1 out of 1 in the Escherichia Coli Rna Polymerase and RRNBP1 Promoter Closed Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Escherichia Coli Rna Polymerase and RRNBP1 Promoter Closed Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg2001

b:46.3
occ:1.00
OD2 D:ASP464 2.0 39.9 1.0
OD1 D:ASP464 2.2 39.9 1.0
OD1 D:ASP462 2.3 42.8 1.0
CG D:ASP464 2.4 39.9 1.0
CG D:ASP462 3.1 42.8 1.0
OD2 D:ASP462 3.2 42.8 1.0
CB D:ASP460 3.2 37.4 1.0
O D:ASP460 3.6 37.4 1.0
NH2 D:ARG425 3.8 29.6 1.0
CB D:ASP464 3.8 39.9 1.0
CA D:ASP460 4.0 37.4 1.0
N D:ASP460 4.0 37.4 1.0
C D:ASP460 4.1 37.4 1.0
CG D:ASP460 4.2 37.4 1.0
CB D:ASP462 4.5 42.8 1.0
OD2 D:ASP460 4.6 37.4 1.0
N D:ASP464 4.6 39.9 1.0
CA D:ASP464 4.7 39.9 1.0
N D:ASP462 4.7 42.8 1.0
O D:ASP462 4.8 42.8 1.0
C D:ASP462 4.9 42.8 1.0
CZ D:ARG425 4.9 29.6 1.0
CA D:ASP462 5.0 42.8 1.0

Reference:

Y.Shin, M.Z.Qayyum, K.S.Murakami. Escherichia Coli Rna Polymerase and RRNBP1 Promoter Closed Complex To Be Published.
Page generated: Tue Dec 15 03:45:09 2020

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