Magnesium in PDB 6x4y: Mfd-Bound E.Coli Rna Polymerase Elongation Complex - IV State

Enzymatic activity of Mfd-Bound E.Coli Rna Polymerase Elongation Complex - IV State

All present enzymatic activity of Mfd-Bound E.Coli Rna Polymerase Elongation Complex - IV State:
2.7.7.6;

Other elements in 6x4y:

The structure of Mfd-Bound E.Coli Rna Polymerase Elongation Complex - IV State also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Mfd-Bound E.Coli Rna Polymerase Elongation Complex - IV State (pdb code 6x4y). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Mfd-Bound E.Coli Rna Polymerase Elongation Complex - IV State, PDB code: 6x4y:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 6x4y

Go back to Magnesium Binding Sites List in 6x4y
Magnesium binding site 1 out of 2 in the Mfd-Bound E.Coli Rna Polymerase Elongation Complex - IV State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Mfd-Bound E.Coli Rna Polymerase Elongation Complex - IV State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2001

b:45.0
occ:1.00
OD2 A:ASP729 3.1 49.8 1.0
OD1 A:ASP729 3.4 49.8 1.0
O3A A:ADP2000 3.4 81.0 1.0
O3B A:ADP2000 3.5 81.0 1.0
CG A:ASP729 3.6 49.8 1.0
OG1 A:THR635 3.6 70.4 1.0
CE1 A:HIS665 4.0 62.5 1.0
NE2 A:HIS665 4.1 62.5 1.0
PB A:ADP2000 4.2 81.0 1.0
PA A:ADP2000 4.5 81.0 1.0
O1A A:ADP2000 4.6 81.0 1.0
CD1 A:LEU661 4.8 60.0 1.0
O2A A:ADP2000 4.9 81.0 1.0

Magnesium binding site 2 out of 2 in 6x4y

Go back to Magnesium Binding Sites List in 6x4y
Magnesium binding site 2 out of 2 in the Mfd-Bound E.Coli Rna Polymerase Elongation Complex - IV State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Mfd-Bound E.Coli Rna Polymerase Elongation Complex - IV State within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Mg1501

b:54.2
occ:1.00
O3' R:A20 2.0 72.3 1.0
OD1 J:ASP460 2.0 44.9 1.0
OD1 J:ASP464 2.0 53.8 1.0
O2' R:A20 2.4 72.3 1.0
OD2 J:ASP464 2.6 53.8 1.0
CG J:ASP464 2.6 53.8 1.0
C3' R:A20 2.9 72.3 1.0
CG J:ASP460 3.0 44.9 1.0
C2' R:A20 3.1 72.3 1.0
OD2 J:ASP460 3.2 44.9 1.0
OD1 J:ASP462 3.2 45.8 1.0
NH2 J:ARG425 3.3 72.3 1.0
C4' R:A20 3.6 72.3 1.0
O J:ASP460 4.1 44.9 1.0
CB J:ASP464 4.1 53.8 1.0
N J:ASP460 4.3 44.9 1.0
CG J:ASP462 4.3 45.8 1.0
CB J:ASP460 4.3 44.9 1.0
C1' R:A20 4.4 72.3 1.0
CZ J:ARG425 4.4 72.3 1.0
O4' R:A20 4.5 72.3 1.0
C5' R:A20 4.6 72.3 1.0
C J:ASP460 4.6 44.9 1.0
CA J:ASP460 4.7 44.9 1.0
OD2 J:ASP462 4.7 45.8 1.0
CA J:ASP464 4.7 53.8 1.0
NE J:ARG425 4.7 72.3 1.0
N J:ASP464 4.8 53.8 1.0

Reference:

J.Y.Kang, E.Llewellyn, J.Chen, P.D.B.Olinares, J.Brewer, B.T.Chait, E.A.Campbell, S.A.Darst. Structural Basis For Transcription Complex Disruption By the Mfd Translocase. Elife V. 10 2021.
ISSN: ESSN 2050-084X
PubMed: 33480355
DOI: 10.7554/ELIFE.62117
Page generated: Wed Mar 3 14:57:44 2021

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