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Magnesium in PDB 2yu9: Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Utp

Enzymatic activity of Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Utp

All present enzymatic activity of Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Utp:
2.7.7.6;

Protein crystallography data

The structure of Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Utp, PDB code: 2yu9 was solved by D.Wang, D.A.Bushnell, K.D.Westover, C.D.Kaplan, R.D.Kornberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.98 / 3.40
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 170.610, 222.729, 196.160, 90.00, 101.87, 90.00
R / Rfree (%) 28.3 / 34.4

Other elements in 2yu9:

The structure of Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Utp also contains other interesting chemical elements:

Zinc (Zn) 8 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Utp (pdb code 2yu9). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Utp, PDB code: 2yu9:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 2yu9

Go back to Magnesium Binding Sites List in 2yu9
Magnesium binding site 1 out of 2 in the Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Utp


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 in 150 Mm Mg+2 with Utp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2001

b:0.7
occ:1.00
OD2 A:ASP485 2.1 0.8 1.0
OD2 A:ASP483 2.2 0.4 1.0
OD1 A:ASP485 2.3 0.8 1.0
CG A:ASP485 2.3 0.9 1.0
OD1 A:ASP481 2.4 1.0 1.0
CG A:ASP483 3.0 0.9 1.0
CG A:ASP481 3.1 0.7 1.0
OD1 A:ASP483 3.1 0.8 1.0
OD2 A:ASP481 3.2 0.9 1.0
O2A A:UTP2003 3.4 0.4 0.3
CB A:ASP485 3.5 0.8 1.0
O1A A:UTP2003 3.8 0.4 0.3
O2G A:UTP2003 3.8 0.1 0.7
C4' R:A10 4.0 0.4 1.0
PA A:UTP2003 4.0 0.4 0.3
C3' R:A10 4.0 0.9 1.0
N A:ASP481 4.2 0.3 1.0
NH2 A:ARG446 4.3 0.1 1.0
C5' A:UTP2003 4.3 0.4 0.3
CA A:ASP485 4.3 0.0 1.0
N A:ASP485 4.3 0.3 1.0
O2' R:A10 4.4 0.3 1.0
CB A:ASP481 4.4 0.2 1.0
N A:ASP483 4.5 0.6 1.0
CB A:ASP483 4.5 0.9 1.0
C5' R:A10 4.5 0.7 1.0
C A:ASP481 4.6 0.6 1.0
O A:ASP481 4.6 0.7 1.0
O5' A:UTP2003 4.7 0.4 0.3
CA A:ASP481 4.7 0.7 1.0
C2' R:A10 4.8 0.5 1.0
CA A:ASP483 4.9 0.4 1.0
O2A A:UTP2003 5.0 0.1 0.7
O4' A:UTP2003 5.0 0.4 0.3
N A:PHE482 5.0 0.1 1.0

Magnesium binding site 2 out of 2 in 2yu9

Go back to Magnesium Binding Sites List in 2yu9
Magnesium binding site 2 out of 2 in the Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Utp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Utp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2002

b:59.7
occ:1.00
O1G A:UTP2003 1.6 0.4 0.3
C6 A:UTP2003 2.6 0.9 0.7
PG A:UTP2003 2.6 0.4 0.3
C5 A:UTP2003 3.1 0.4 0.7
OD2 A:ASP481 3.1 0.9 1.0
O3B A:UTP2003 3.1 0.4 0.3
O3G A:UTP2003 3.3 0.4 0.3
O5' A:UTP2003 3.5 0.8 0.7
O4' A:UTP2003 3.6 0.1 0.7
N1 A:UTP2003 3.7 0.6 0.7
O2A A:UTP2003 3.9 0.4 0.3
C5' A:UTP2003 3.9 0.2 0.7
CG A:ASP481 4.0 0.7 1.0
CB A:ASP481 4.0 0.2 1.0
O2G A:UTP2003 4.1 0.4 0.3
O3A A:UTP2003 4.1 0.6 0.7
C1' A:UTP2003 4.1 0.5 0.7
O2A A:UTP2003 4.2 0.1 0.7
PA A:UTP2003 4.3 0.1 0.7
C4' A:UTP2003 4.3 0.6 0.7
OE1 B:GLU836 4.3 0.3 1.0
O5' A:UTP2003 4.3 0.4 0.3
C4 A:UTP2003 4.4 0.3 0.7
PB A:UTP2003 4.5 0.4 0.3
O2G A:UTP2003 4.5 0.1 0.7
O1B A:UTP2003 4.6 0.4 0.3
NH2 B:ARG1020 4.7 0.3 1.0
C5' A:UTP2003 4.7 0.4 0.3
PA A:UTP2003 4.7 0.4 0.3
C2 A:UTP2003 4.9 0.3 0.7
N A:ASP481 5.0 0.3 1.0

Reference:

D.Wang, D.A.Bushnell, K.D.Westover, C.D.Kaplan, R.D.Kornberg. Structural Basis of Transcription: Role of the Trigger Loop in Substrate Specificity and Catalysis Cell(Cambridge,Mass.) V. 127 941 2006.
ISSN: ISSN 0092-8674
PubMed: 17129781
DOI: 10.1016/J.CELL.2006.11.023
Page generated: Mon Dec 14 07:49:32 2020

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