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Magnesium in PDB 5m3f: Yeast Rna Polymerase I Elongation Complex at 3.8A

Enzymatic activity of Yeast Rna Polymerase I Elongation Complex at 3.8A

All present enzymatic activity of Yeast Rna Polymerase I Elongation Complex at 3.8A:
2.7.7.6;

Other elements in 5m3f:

The structure of Yeast Rna Polymerase I Elongation Complex at 3.8A also contains other interesting chemical elements:

Zinc (Zn) 6 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Yeast Rna Polymerase I Elongation Complex at 3.8A (pdb code 5m3f). 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 Yeast Rna Polymerase I Elongation Complex at 3.8A, PDB code: 5m3f:

Magnesium binding site 1 out of 1 in 5m3f

Go back to Magnesium Binding Sites List in 5m3f
Magnesium binding site 1 out of 1 in the Yeast Rna Polymerase I Elongation Complex at 3.8A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Yeast Rna Polymerase I Elongation Complex at 3.8A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg3003

b:30.0
occ:1.00
OD1 A:ASP629 2.4 66.9 1.0
OD1 A:ASP631 2.6 83.2 1.0
OD2 A:ASP627 2.7 89.0 1.0
CB A:ASP627 2.9 61.8 1.0
CG A:ASP629 3.1 65.2 1.0
CG A:ASP627 3.2 76.2 1.0
OD2 A:ASP629 3.2 61.3 1.0
O3' R:C20 3.4 0.6 1.0
O2' R:C20 3.4 0.6 1.0
CG A:ASP631 3.4 68.0 1.0
C4' R:C20 3.5 0.6 1.0
OD2 A:ASP631 3.7 60.5 1.0
C3' R:C20 3.9 0.6 1.0
CA A:ASP627 4.1 54.5 1.0
N A:ASP627 4.2 59.0 1.0
C5' R:C20 4.2 0.6 1.0
C2' R:C20 4.2 0.6 1.0
OD1 A:ASP627 4.3 78.2 1.0
CB A:ASP629 4.5 58.9 1.0
O4' R:C20 4.5 0.6 1.0
N A:ASP631 4.6 46.8 1.0
CB A:ASP631 4.7 58.0 1.0
N A:ASP629 4.7 49.2 1.0
C A:ASP627 4.8 56.7 1.0
C1' R:C20 4.9 0.6 1.0
CA A:ASP631 5.0 47.8 1.0
CA A:ASP629 5.0 49.9 1.0

Reference:

S.Neyer, M.Kunz, C.Geiss, M.Hantsche, V.V.Hodirnau, A.Seybert, C.Engel, M.P.Scheffer, P.Cramer, A.S.Frangakis. Structure of Rna Polymerase I Transcribing Ribosomal Dna Genes. Nature V. 540 607 2016.
ISSN: ISSN 0028-0836
PubMed: 27842382
DOI: 10.1038/NATURE20561
Page generated: Mon Dec 14 20:50:12 2020

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