Atomistry » Manganese » PDB 1ss9-1uvi » 1twc
Atomistry »
  Manganese »
    PDB 1ss9-1uvi »
      1twc »

Manganese in PDB 1twc: Rna Polymerase II Complexed with Gtp

Enzymatic activity of Rna Polymerase II Complexed with Gtp

All present enzymatic activity of Rna Polymerase II Complexed with Gtp:
2.7.7.6;

Protein crystallography data

The structure of Rna Polymerase II Complexed with Gtp, PDB code: 1twc was solved by K.D.Westover, D.A.Bushnell, R.D.Kornberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 3.00
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 123.226, 223.613, 374.610, 90.00, 90.00, 90.00
R / Rfree (%) 23.4 / 25.5

Other elements in 1twc:

The structure of Rna Polymerase II Complexed with Gtp also contains other interesting chemical elements:

Zinc (Zn) 8 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Rna Polymerase II Complexed with Gtp (pdb code 1twc). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Rna Polymerase II Complexed with Gtp, PDB code: 1twc:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 1twc

Go back to Manganese Binding Sites List in 1twc
Manganese binding site 1 out of 2 in the Rna Polymerase II Complexed with Gtp


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Rna Polymerase II Complexed with Gtp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn3009

b:36.2
occ:1.00
OD1 A:ASP481 1.8 33.3 1.0
O2G B:GTP3008 2.0 96.7 1.0
OD2 A:ASP483 2.0 27.9 1.0
OD2 A:ASP485 2.2 30.4 1.0
O1B B:GTP3008 2.4 97.3 1.0
CG A:ASP481 2.9 29.3 1.0
CG A:ASP483 3.0 28.1 1.0
CG A:ASP485 3.2 28.5 1.0
OD2 A:ASP481 3.2 30.2 1.0
PB B:GTP3008 3.2 97.8 1.0
O2B B:GTP3008 3.3 98.3 1.0
PG B:GTP3008 3.3 98.2 1.0
OD1 A:ASP483 3.3 31.9 1.0
OD1 A:ASP485 3.5 29.1 1.0
O3B B:GTP3008 3.7 98.3 1.0
MN A:MN3010 3.9 48.0 1.0
O1G B:GTP3008 4.2 98.5 1.0
O3G B:GTP3008 4.3 98.4 1.0
CB A:ASP483 4.3 26.1 1.0
CB A:ASP485 4.5 26.3 1.0
O A:ASP481 4.6 26.9 1.0
N A:ASP485 4.6 25.7 1.0
N A:ASP483 4.6 27.1 1.0
N A:ASP481 4.6 25.6 1.0
CB A:ASP481 4.6 25.3 1.0
C A:ASP481 4.7 26.1 1.0
O3A B:GTP3008 4.7 99.0 1.0
C A:ASP483 4.8 26.0 1.0
CA A:ASP483 4.8 26.3 1.0
NZ B:LYS987 4.9 53.9 1.0
O A:ASP483 4.9 25.6 1.0
CA A:ASP481 4.9 25.8 1.0
CA A:ASP485 5.0 25.9 1.0

Manganese binding site 2 out of 2 in 1twc

Go back to Manganese Binding Sites List in 1twc
Manganese binding site 2 out of 2 in the Rna Polymerase II Complexed with Gtp


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Rna Polymerase II Complexed with Gtp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn3010

b:48.0
occ:1.00
O1B B:GTP3008 2.1 97.3 1.0
OD2 B:ASP837 2.4 38.6 1.0
OD1 A:ASP483 2.4 31.9 1.0
OD2 A:ASP481 2.5 30.2 1.0
O1A B:GTP3008 2.5 99.6 1.0
PB B:GTP3008 3.1 97.8 1.0
O3A B:GTP3008 3.2 99.0 1.0
PA B:GTP3008 3.4 99.8 1.0
CG A:ASP483 3.4 28.1 1.0
CG B:ASP837 3.5 37.2 1.0
NE2 B:GLN986 3.7 62.5 1.0
CG A:ASP481 3.8 29.3 1.0
OD2 A:ASP483 3.8 27.9 1.0
MN A:MN3009 3.9 36.2 1.0
CB B:ASP837 4.0 34.9 1.0
NH2 B:ARG1020 4.0 51.4 1.0
O2A B:GTP3008 4.1 0.6 1.0
O2B B:GTP3008 4.1 98.3 1.0
OD1 A:ASP481 4.2 33.3 1.0
O3B B:GTP3008 4.3 98.3 1.0
OE1 B:GLN986 4.3 63.9 1.0
CB A:ASP483 4.3 26.1 1.0
CD B:GLN986 4.4 59.8 1.0
OD1 B:ASP837 4.4 36.7 1.0
O5' B:GTP3008 4.7 0.7 1.0
O2G B:GTP3008 4.9 96.7 1.0

Reference:

K.D.Westover, D.A.Bushnell, R.D.Kornberg. Structural Basis of Transcription: Nucleotide Selection By Rotation in the Rna Polymerase II Active Center. Cell(Cambridge,Mass.) V. 119 481 2004.
ISSN: ISSN 0092-8674
PubMed: 15537538
DOI: 10.1016/J.CELL.2004.10.016
Page generated: Sat Oct 5 12:36:46 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy