Zinc in PDB 2nvt: Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Gmpcpp
Enzymatic activity of Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Gmpcpp
All present enzymatic activity of Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Gmpcpp:
2.7.7.6;
Protein crystallography data
The structure of Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Gmpcpp, PDB code: 2nvt
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)
|
40.00 /
3.36
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
170.872,
222.824,
195.802,
90.00,
102.39,
90.00
|
R / Rfree (%)
|
23 /
28.3
|
Other elements in 2nvt:
The structure of Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Gmpcpp also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Gmpcpp
(pdb code 2nvt). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 8 binding sites of Zinc where determined in the
Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Gmpcpp, PDB code: 2nvt:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Zinc binding site 1 out
of 8 in 2nvt
Go back to
Zinc Binding Sites List in 2nvt
Zinc binding site 1 out
of 8 in the Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Gmpcpp
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Gmpcpp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1734
b:0.6
occ:1.00
|
SG
|
A:CYS107
|
2.4
|
0.7
|
1.0
|
SG
|
A:CYS148
|
2.4
|
0.8
|
1.0
|
SG
|
A:CYS110
|
2.4
|
0.9
|
1.0
|
SG
|
A:CYS167
|
2.4
|
0.4
|
1.0
|
O
|
A:CYS167
|
3.3
|
0.6
|
1.0
|
CB
|
A:CYS107
|
3.5
|
0.1
|
1.0
|
CB
|
A:CYS110
|
3.5
|
0.1
|
1.0
|
CB
|
A:CYS148
|
3.6
|
0.7
|
1.0
|
N
|
A:CYS167
|
3.7
|
0.6
|
1.0
|
CB
|
A:CYS167
|
3.7
|
0.8
|
1.0
|
C
|
A:CYS167
|
3.9
|
0.6
|
1.0
|
CA
|
A:CYS167
|
3.9
|
0.1
|
1.0
|
N
|
A:CYS110
|
4.6
|
0.1
|
1.0
|
CA
|
A:CYS110
|
4.6
|
0.7
|
1.0
|
C
|
A:GLY166
|
4.7
|
0.1
|
1.0
|
O
|
A:MET108
|
4.7
|
0.7
|
1.0
|
CA
|
A:CYS107
|
4.9
|
0.7
|
1.0
|
ND2
|
A:ASN169
|
4.9
|
0.7
|
1.0
|
N
|
A:GLY168
|
5.0
|
0.0
|
1.0
|
|
Zinc binding site 2 out
of 8 in 2nvt
Go back to
Zinc Binding Sites List in 2nvt
Zinc binding site 2 out
of 8 in the Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Gmpcpp
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Gmpcpp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1735
b:0.2
occ:1.00
|
SG
|
A:CYS70
|
2.3
|
0.1
|
1.0
|
SG
|
A:CYS67
|
2.3
|
0.1
|
1.0
|
SG
|
A:CYS77
|
2.3
|
0.5
|
1.0
|
NE2
|
A:HIS80
|
2.5
|
0.5
|
1.0
|
CD2
|
A:HIS80
|
3.1
|
0.5
|
1.0
|
NE2
|
A:GLN68
|
3.1
|
0.2
|
1.0
|
CB
|
A:CYS70
|
3.3
|
0.5
|
1.0
|
CB
|
A:CYS77
|
3.3
|
0.2
|
1.0
|
CB
|
A:CYS67
|
3.4
|
0.1
|
1.0
|
CE1
|
A:HIS80
|
3.6
|
0.3
|
1.0
|
O
|
A:CYS67
|
3.7
|
0.4
|
1.0
|
CD
|
A:GLN68
|
4.1
|
0.8
|
1.0
|
CA
|
A:CYS77
|
4.1
|
0.1
|
1.0
|
CG
|
A:HIS80
|
4.4
|
0.7
|
1.0
|
C
|
A:CYS67
|
4.4
|
0.3
|
1.0
|
CA
|
A:CYS67
|
4.4
|
0.3
|
1.0
|
ND1
|
A:HIS80
|
4.6
|
0.1
|
1.0
|
CA
|
A:CYS70
|
4.7
|
0.7
|
1.0
|
OE1
|
A:GLN68
|
4.7
|
0.5
|
1.0
|
C
|
A:CYS70
|
4.9
|
0.5
|
1.0
|
CB
|
A:GLU72
|
5.0
|
0.6
|
1.0
|
|
Zinc binding site 3 out
of 8 in 2nvt
Go back to
Zinc Binding Sites List in 2nvt
Zinc binding site 3 out
of 8 in the Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Gmpcpp
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Gmpcpp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn1307
b:0.3
occ:1.00
|
SG
|
B:CYS1166
|
2.3
|
0.3
|
1.0
|
SG
|
B:CYS1163
|
2.3
|
0.8
|
1.0
|
SG
|
B:CYS1185
|
2.4
|
0.3
|
1.0
|
SG
|
B:CYS1182
|
2.4
|
1.0
|
1.0
|
CB
|
B:CYS1163
|
3.4
|
0.2
|
1.0
|
CB
|
B:CYS1166
|
3.5
|
0.8
|
1.0
|
CB
|
B:CYS1185
|
3.5
|
0.3
|
1.0
|
CB
|
B:CYS1182
|
3.6
|
0.0
|
1.0
|
N
|
B:CYS1166
|
3.9
|
1.0
|
1.0
|
CA
|
B:CYS1166
|
4.3
|
0.6
|
1.0
|
O
|
B:CYS1182
|
4.6
|
0.7
|
1.0
|
CA
|
B:CYS1185
|
4.6
|
0.2
|
1.0
|
CB
|
B:ILE1165
|
4.6
|
0.5
|
1.0
|
N
|
B:CYS1185
|
4.7
|
0.8
|
1.0
|
CA
|
B:CYS1163
|
4.7
|
0.8
|
1.0
|
CD1
|
A:ILE30
|
4.8
|
0.7
|
1.0
|
OG1
|
B:THR1170
|
4.9
|
0.1
|
1.0
|
N
|
B:GLY1167
|
4.9
|
0.4
|
1.0
|
CA
|
B:CYS1182
|
4.9
|
1.0
|
1.0
|
|
Zinc binding site 4 out
of 8 in 2nvt
Go back to
Zinc Binding Sites List in 2nvt
Zinc binding site 4 out
of 8 in the Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Gmpcpp
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Gmpcpp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn319
b:0.5
occ:1.00
|
SG
|
C:CYS88
|
2.3
|
0.7
|
1.0
|
SG
|
C:CYS86
|
2.3
|
0.6
|
1.0
|
SG
|
C:CYS95
|
2.3
|
0.6
|
1.0
|
SG
|
C:CYS92
|
2.4
|
0.2
|
1.0
|
N
|
C:CYS92
|
2.9
|
0.3
|
1.0
|
CB
|
C:CYS95
|
3.3
|
0.5
|
1.0
|
CB
|
C:CYS88
|
3.4
|
0.3
|
1.0
|
CB
|
C:CYS92
|
3.5
|
0.3
|
1.0
|
CB
|
C:CYS86
|
3.5
|
0.5
|
1.0
|
CA
|
C:CYS92
|
3.6
|
0.3
|
1.0
|
C
|
C:HIS91
|
3.7
|
0.6
|
1.0
|
N
|
C:CYS95
|
3.8
|
0.8
|
1.0
|
CA
|
C:HIS91
|
4.0
|
0.7
|
1.0
|
C
|
C:CYS92
|
4.1
|
0.3
|
1.0
|
CA
|
C:CYS95
|
4.2
|
0.3
|
1.0
|
O
|
C:CYS92
|
4.2
|
0.5
|
1.0
|
CA
|
C:CYS88
|
4.6
|
0.7
|
1.0
|
O
|
C:HIS91
|
4.7
|
0.8
|
1.0
|
C
|
C:LYS94
|
4.7
|
0.3
|
1.0
|
CB
|
C:LYS94
|
4.7
|
0.4
|
1.0
|
N
|
C:CYS88
|
4.7
|
0.2
|
1.0
|
N
|
C:LYS94
|
4.7
|
0.4
|
1.0
|
O
|
C:CYS88
|
4.8
|
0.9
|
1.0
|
CA
|
C:CYS86
|
4.9
|
0.5
|
1.0
|
O
|
C:ASP90
|
4.9
|
0.3
|
1.0
|
N
|
C:HIS91
|
4.9
|
0.1
|
1.0
|
CB
|
C:HIS91
|
4.9
|
0.6
|
1.0
|
CA
|
C:LYS94
|
4.9
|
0.6
|
1.0
|
C
|
C:CYS95
|
5.0
|
0.3
|
1.0
|
N
|
C:ASP93
|
5.0
|
1.0
|
1.0
|
|
Zinc binding site 5 out
of 8 in 2nvt
Go back to
Zinc Binding Sites List in 2nvt
Zinc binding site 5 out
of 8 in the Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Gmpcpp
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Gmpcpp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:Zn203
b:0.4
occ:1.00
|
SG
|
I:CYS10
|
2.3
|
0.7
|
1.0
|
SG
|
I:CYS7
|
2.3
|
0.1
|
1.0
|
SG
|
I:CYS29
|
2.3
|
0.2
|
1.0
|
SG
|
I:CYS32
|
2.4
|
0.6
|
1.0
|
CB
|
I:CYS10
|
3.1
|
0.2
|
1.0
|
CB
|
I:CYS7
|
3.2
|
0.5
|
1.0
|
N
|
I:CYS32
|
3.3
|
0.8
|
1.0
|
CB
|
I:CYS29
|
3.4
|
0.1
|
1.0
|
CB
|
I:CYS32
|
3.5
|
1.0
|
1.0
|
CB
|
I:THR31
|
3.8
|
0.5
|
1.0
|
OG1
|
I:THR31
|
3.8
|
0.2
|
1.0
|
N
|
I:CYS10
|
3.9
|
0.1
|
1.0
|
CA
|
I:CYS32
|
3.9
|
0.6
|
1.0
|
CA
|
I:CYS10
|
4.0
|
0.1
|
1.0
|
CB
|
I:TYR34
|
4.2
|
0.4
|
1.0
|
C
|
I:THR31
|
4.3
|
0.1
|
1.0
|
CA
|
I:THR31
|
4.5
|
0.3
|
1.0
|
N
|
I:THR31
|
4.5
|
0.2
|
1.0
|
C
|
I:CYS32
|
4.5
|
0.8
|
1.0
|
CA
|
I:CYS7
|
4.6
|
0.6
|
1.0
|
N
|
I:TYR34
|
4.8
|
0.0
|
1.0
|
CA
|
I:CYS29
|
4.8
|
0.8
|
1.0
|
C
|
I:ASP9
|
4.8
|
0.1
|
1.0
|
N
|
I:SER33
|
4.9
|
0.6
|
1.0
|
|
Zinc binding site 6 out
of 8 in 2nvt
Go back to
Zinc Binding Sites List in 2nvt
Zinc binding site 6 out
of 8 in the Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Gmpcpp
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 6 of Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Gmpcpp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:Zn204
b:1.0
occ:1.00
|
SG
|
I:CYS103
|
2.3
|
0.7
|
1.0
|
SG
|
I:CYS78
|
2.3
|
0.8
|
1.0
|
SG
|
I:CYS106
|
2.4
|
0.4
|
1.0
|
SG
|
I:CYS75
|
2.4
|
0.6
|
1.0
|
O
|
I:CYS78
|
3.0
|
0.2
|
1.0
|
CB
|
I:CYS106
|
3.3
|
0.5
|
1.0
|
CB
|
I:CYS75
|
3.3
|
0.8
|
1.0
|
CB
|
I:CYS78
|
3.4
|
0.5
|
1.0
|
CB
|
I:CYS103
|
3.4
|
0.4
|
1.0
|
C
|
I:CYS78
|
3.8
|
1.0
|
1.0
|
CA
|
I:CYS78
|
4.0
|
0.3
|
1.0
|
N
|
I:CYS78
|
4.1
|
0.6
|
1.0
|
N
|
I:CYS106
|
4.2
|
0.7
|
1.0
|
CA
|
I:CYS106
|
4.4
|
0.4
|
1.0
|
CB
|
I:HIS108
|
4.5
|
0.7
|
1.0
|
CB
|
I:SER105
|
4.5
|
0.6
|
1.0
|
CG
|
I:LYS77
|
4.5
|
1.0
|
1.0
|
C
|
I:SER105
|
4.5
|
0.0
|
1.0
|
CA
|
I:CYS75
|
4.7
|
0.7
|
1.0
|
O
|
I:CYS75
|
4.7
|
0.6
|
1.0
|
CA
|
I:CYS103
|
4.8
|
0.9
|
1.0
|
C
|
I:CYS75
|
4.9
|
0.4
|
1.0
|
O
|
I:SER80
|
4.9
|
0.8
|
1.0
|
CA
|
I:SER105
|
4.9
|
0.7
|
1.0
|
|
Zinc binding site 7 out
of 8 in 2nvt
Go back to
Zinc Binding Sites List in 2nvt
Zinc binding site 7 out
of 8 in the Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Gmpcpp
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 7 of Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Gmpcpp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
J:Zn101
b:1.0
occ:1.00
|
SG
|
J:CYS46
|
2.3
|
0.2
|
1.0
|
SG
|
J:CYS10
|
2.3
|
0.8
|
1.0
|
SG
|
J:CYS45
|
2.4
|
0.9
|
1.0
|
SG
|
J:CYS7
|
2.4
|
0.9
|
1.0
|
N
|
J:CYS46
|
2.8
|
0.5
|
1.0
|
C
|
J:CYS45
|
3.3
|
0.6
|
1.0
|
CB
|
J:CYS46
|
3.3
|
0.6
|
1.0
|
CB
|
J:CYS10
|
3.3
|
0.8
|
1.0
|
CA
|
J:CYS46
|
3.3
|
0.1
|
1.0
|
CB
|
J:CYS45
|
3.4
|
0.3
|
1.0
|
CB
|
J:CYS7
|
3.5
|
0.0
|
1.0
|
N
|
J:CYS10
|
3.7
|
0.8
|
1.0
|
CG
|
J:ARG43
|
3.8
|
0.1
|
1.0
|
O
|
J:CYS45
|
3.9
|
1.0
|
1.0
|
OG
|
J:SER9
|
3.9
|
0.1
|
1.0
|
CA
|
J:CYS45
|
3.9
|
1.0
|
1.0
|
CA
|
J:CYS10
|
4.1
|
1.0
|
1.0
|
CD
|
J:ARG43
|
4.2
|
0.4
|
1.0
|
O
|
J:ARG43
|
4.3
|
0.5
|
1.0
|
N
|
J:CYS45
|
4.5
|
0.8
|
1.0
|
C
|
J:SER9
|
4.7
|
0.4
|
1.0
|
CB
|
J:SER9
|
4.7
|
0.1
|
1.0
|
C
|
J:CYS46
|
4.8
|
0.0
|
1.0
|
CA
|
J:CYS7
|
4.9
|
0.3
|
1.0
|
CB
|
J:ARG43
|
4.9
|
0.0
|
1.0
|
|
Zinc binding site 8 out
of 8 in 2nvt
Go back to
Zinc Binding Sites List in 2nvt
Zinc binding site 8 out
of 8 in the Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Gmpcpp
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 8 of Rna Polymerase II Elongation Complex in 150 Mm Mg+2 with Gmpcpp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
L:Zn105
b:0.8
occ:1.00
|
SG
|
L:CYS48
|
2.3
|
0.3
|
1.0
|
SG
|
L:CYS31
|
2.3
|
0.9
|
1.0
|
SG
|
L:CYS51
|
2.4
|
0.2
|
1.0
|
SG
|
L:CYS34
|
2.4
|
0.8
|
1.0
|
CB
|
L:CYS31
|
3.3
|
0.9
|
1.0
|
CB
|
L:CYS48
|
3.4
|
0.5
|
1.0
|
CB
|
L:CYS51
|
3.5
|
0.7
|
1.0
|
CB
|
L:CYS34
|
3.5
|
0.1
|
1.0
|
N
|
L:CYS51
|
4.0
|
0.8
|
1.0
|
N
|
L:GLY52
|
4.1
|
0.7
|
1.0
|
CA
|
L:CYS51
|
4.1
|
0.3
|
1.0
|
C
|
L:CYS51
|
4.5
|
0.1
|
1.0
|
N
|
L:LYS49
|
4.6
|
1.0
|
1.0
|
CA
|
L:CYS34
|
4.6
|
0.4
|
1.0
|
N
|
L:CYS34
|
4.7
|
0.8
|
1.0
|
CA
|
L:CYS31
|
4.7
|
0.7
|
1.0
|
CB
|
L:SER36
|
4.7
|
0.6
|
1.0
|
CA
|
L:CYS48
|
4.8
|
0.7
|
1.0
|
N
|
L:ASP50
|
4.8
|
0.5
|
1.0
|
C
|
L:ASP50
|
4.9
|
0.4
|
1.0
|
N
|
L:HIS53
|
5.0
|
0.1
|
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: Thu Oct 17 02:17:57 2024
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