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Magnesium in PDB 7wbx: Rna Polymerase II Elongation Complex Bound with ELF1 and SPT4/5, Stalled at Shl(-3) of the Nucleosome

Enzymatic activity of Rna Polymerase II Elongation Complex Bound with ELF1 and SPT4/5, Stalled at Shl(-3) of the Nucleosome

All present enzymatic activity of Rna Polymerase II Elongation Complex Bound with ELF1 and SPT4/5, Stalled at Shl(-3) of the Nucleosome:
2.7.7.6;

Other elements in 7wbx:

The structure of Rna Polymerase II Elongation Complex Bound with ELF1 and SPT4/5, Stalled at Shl(-3) of the Nucleosome also contains other interesting chemical elements:

Zinc (Zn) 10 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Rna Polymerase II Elongation Complex Bound with ELF1 and SPT4/5, Stalled at Shl(-3) of the Nucleosome (pdb code 7wbx). 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 Rna Polymerase II Elongation Complex Bound with ELF1 and SPT4/5, Stalled at Shl(-3) of the Nucleosome, PDB code: 7wbx:

Magnesium binding site 1 out of 1 in 7wbx

Go back to Magnesium Binding Sites List in 7wbx
Magnesium binding site 1 out of 1 in the Rna Polymerase II Elongation Complex Bound with ELF1 and SPT4/5, Stalled at Shl(-3) of the Nucleosome


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Rna Polymerase II Elongation Complex Bound with ELF1 and SPT4/5, Stalled at Shl(-3) of the Nucleosome within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1803

b:75.8
occ:1.00
O3' P:G10 1.9 74.8 1.0
OD1 A:ASP486 2.0 61.5 1.0
OD1 A:ASP482 2.1 56.5 1.0
OD2 A:ASP486 2.2 61.5 1.0
CG A:ASP486 2.4 61.5 1.0
OD1 A:ASP484 2.8 59.3 1.0
CG A:ASP482 3.0 56.5 1.0
C3' P:G10 3.1 74.8 1.0
O2' P:G10 3.2 74.8 1.0
OD2 A:ASP482 3.2 56.5 1.0
HH21 A:ARG447 3.5 57.0 1.0
H4' P:G10 3.5 74.8 1.0
H A:ASP482 3.6 56.5 1.0
CG A:ASP484 3.6 59.3 1.0
HO2' P:G10 3.7 74.8 1.0
OD2 A:ASP484 3.7 59.3 1.0
C2' P:G10 3.7 74.8 1.0
C4' P:G10 3.8 74.8 1.0
H3' P:G10 3.8 74.8 1.0
CB A:ASP486 3.9 61.5 1.0
HH22 A:ARG447 3.9 57.0 1.0
NH2 A:ARG447 3.9 57.0 1.0
H2' P:G10 4.1 74.8 1.0
O A:ASP482 4.1 56.5 1.0
H5'' P:G10 4.2 74.8 1.0
HB2 A:ASP486 4.2 61.5 1.0
HB3 A:ASP486 4.3 61.5 1.0
N A:ASP482 4.3 56.5 1.0
H A:ASP486 4.4 61.5 1.0
CB A:ASP482 4.4 56.5 1.0
HA A:ASP486 4.5 61.5 1.0
H A:ASP484 4.5 59.3 1.0
CA A:ASP486 4.6 61.5 1.0
C5' P:G10 4.6 74.8 1.0
N A:ASP486 4.6 61.5 1.0
HA A:ALA481 4.7 54.1 1.0
CA A:ASP482 4.7 56.5 1.0
C A:ASP482 4.7 56.5 1.0
HB3 A:ASP482 4.9 56.5 1.0
HB2 A:ASP482 4.9 56.5 1.0
C1' P:G10 5.0 74.8 1.0
O4' P:G10 5.0 74.8 1.0

Reference:

K.Osumi, T.Kujirai, H.Ehara, M.Ogasawara, C.Kinoshita, M.Saotome, W.Kagawa, S.I.Sekine, Y.Takizawa, H.Kurumizaka. Structural Basis of Damaged Nucleotide Recognition By Transcribing Rna Polymerase II in the Nucleosome. J.Mol.Biol. V. 435 68130 2023.
ISSN: ESSN 1089-8638
PubMed: 37120012
DOI: 10.1016/J.JMB.2023.168130
Page generated: Thu Jul 27 19:32:41 2023

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