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Magnesium in PDB 8a40: Structure of Mammalian Pol II-Tfiis Elongation Complex

Enzymatic activity of Structure of Mammalian Pol II-Tfiis Elongation Complex

All present enzymatic activity of Structure of Mammalian Pol II-Tfiis Elongation Complex:
2.7.7.6;

Other elements in 8a40:

The structure of Structure of Mammalian Pol II-Tfiis Elongation Complex also contains other interesting chemical elements:

Zinc (Zn) 11 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Mammalian Pol II-Tfiis Elongation Complex (pdb code 8a40). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Structure of Mammalian Pol II-Tfiis Elongation Complex, PDB code: 8a40:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 8a40

Go back to Magnesium Binding Sites List in 8a40
Magnesium binding site 1 out of 3 in the Structure of Mammalian Pol II-Tfiis Elongation Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Mammalian Pol II-Tfiis Elongation Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2003

b:83.0
occ:1.00
O A:ALA494 3.0 68.1 1.0
O A:THR489 3.6 67.9 1.0
C A:ALA494 3.9 68.1 1.0
N A:ALA494 3.9 68.1 1.0
OE2 B:GLU791 4.1 73.9 1.0
C A:ASN493 4.2 65.4 1.0
OD1 A:ASN493 4.3 65.4 1.0
OG1 A:THR489 4.4 67.9 1.0
C A:THR489 4.4 67.9 1.0
OE1 B:GLU791 4.4 73.9 1.0
CA A:ASN493 4.4 65.4 1.0
CG2 A:THR489 4.5 67.9 1.0
CA A:ALA494 4.5 68.1 1.0
CD B:GLU791 4.6 73.9 1.0
CA A:THR490 4.6 66.5 1.0
MG A:MG2008 4.7 85.1 1.0
N A:ASP495 4.8 73.0 1.0
N A:THR490 4.8 66.5 1.0
O A:ASN493 4.9 65.4 1.0
CB A:ASP495 5.0 73.0 1.0
CB A:THR489 5.0 67.9 1.0

Magnesium binding site 2 out of 3 in 8a40

Go back to Magnesium Binding Sites List in 8a40
Magnesium binding site 2 out of 3 in the Structure of Mammalian Pol II-Tfiis Elongation Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Mammalian Pol II-Tfiis Elongation Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2006

b:73.5
occ:1.00
OD1 A:ASP495 2.1 73.0 1.0
O3' P:U46 2.1 76.8 1.0
OD1 A:ASP497 2.3 70.9 1.0
OD1 A:ASP499 2.6 71.3 1.0
OD2 A:ASP499 2.8 71.3 1.0
CG A:ASP499 2.9 71.3 1.0
CG A:ASP495 3.1 73.0 1.0
CG A:ASP497 3.1 70.9 1.0
OD2 A:ASP497 3.3 70.9 1.0
C3' P:U46 3.3 76.8 1.0
OD2 A:ASP495 3.5 73.0 1.0
O2' P:U46 3.5 76.8 1.0
O A:ASP495 3.7 73.0 1.0
C4' P:U46 3.8 76.8 1.0
C2' P:U46 4.0 76.8 1.0
MG A:MG2008 4.1 85.1 1.0
CB A:ASP499 4.3 71.3 1.0
N A:ASP495 4.3 73.0 1.0
CB A:ASP495 4.4 73.0 1.0
C A:ASP495 4.4 73.0 1.0
C5' P:U46 4.4 76.8 1.0
CA A:ASP495 4.6 73.0 1.0
CB A:ASP497 4.6 70.9 1.0
N A:ASP499 4.7 71.3 1.0
N A:ASP497 4.8 70.9 1.0
CA A:ASP499 4.8 71.3 1.0
NH2 A:ARG460 4.8 66.9 1.0
O4' P:U46 5.0 76.8 1.0

Magnesium binding site 3 out of 3 in 8a40

Go back to Magnesium Binding Sites List in 8a40
Magnesium binding site 3 out of 3 in the Structure of Mammalian Pol II-Tfiis Elongation Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structure of Mammalian Pol II-Tfiis Elongation Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2008

b:85.1
occ:1.00
OD1 A:ASP495 3.1 73.0 1.0
CG A:ASP495 3.3 73.0 1.0
O A:ASN493 3.5 65.4 1.0
OD2 A:ASP495 3.6 73.0 1.0
OD1 A:ASN493 4.0 65.4 1.0
N A:ASP495 4.1 73.0 1.0
MG A:MG2006 4.1 73.5 1.0
C A:ASN493 4.2 65.4 1.0
CB A:ASP495 4.2 73.0 1.0
C A:ALA494 4.2 68.1 1.0
CA A:ALA494 4.4 68.1 1.0
N A:ALA494 4.5 68.1 1.0
OD2 A:ASP499 4.7 71.3 1.0
MG A:MG2003 4.7 83.0 1.0
CG A:ASN493 4.7 65.4 1.0
O A:ALA494 4.7 68.1 1.0
CA A:ASP495 4.8 73.0 1.0
NH2 A:ARG460 4.8 66.9 1.0

Reference:

L.Farnung, M.Ochmann, G.Garg, S.M.Vos, P.Cramer. Structure of A Backtracked Hexasomal Intermediate of Nucleosome Transcription. Mol.Cell V. 82 3126 2022.
ISSN: ISSN 1097-2765
PubMed: 35858621
DOI: 10.1016/J.MOLCEL.2022.06.027
Page generated: Thu Dec 28 07:58:13 2023

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