Zinc in PDB 5ip7: Structure of Rna Polymerase II-TFG1 Peptide Complex
Enzymatic activity of Structure of Rna Polymerase II-TFG1 Peptide Complex
All present enzymatic activity of Structure of Rna Polymerase II-TFG1 Peptide Complex:
2.7.7.6;
Protein crystallography data
The structure of Structure of Rna Polymerase II-TFG1 Peptide Complex, PDB code: 5ip7
was solved by
C.Plaschka,
M.Hantsche,
C.Dienemann,
C.Burzinski,
J.Plitzko,
P.Cramer,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
48.93 /
3.52
|
Space group
|
C 2 2 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
221.220,
392.730,
282.190,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
15.4 /
18
|
Other elements in 5ip7:
The structure of Structure of Rna Polymerase II-TFG1 Peptide Complex also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Structure of Rna Polymerase II-TFG1 Peptide Complex
(pdb code 5ip7). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 8 binding sites of Zinc where determined in the
Structure of Rna Polymerase II-TFG1 Peptide Complex, PDB code: 5ip7:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Zinc binding site 1 out
of 8 in 5ip7
Go back to
Zinc Binding Sites List in 5ip7
Zinc binding site 1 out
of 8 in the Structure of Rna Polymerase II-TFG1 Peptide Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Structure of Rna Polymerase II-TFG1 Peptide Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1801
b:0.6
occ:1.00
|
SG
|
A:CYS148
|
2.3
|
0.9
|
1.0
|
SG
|
A:CYS110
|
2.3
|
0.3
|
1.0
|
SG
|
A:CYS107
|
2.3
|
0.1
|
1.0
|
SG
|
A:CYS167
|
2.4
|
0.7
|
1.0
|
CB
|
A:CYS107
|
3.1
|
0.3
|
1.0
|
CB
|
A:CYS148
|
3.2
|
0.3
|
1.0
|
CB
|
A:CYS110
|
3.2
|
0.4
|
1.0
|
N
|
A:CYS110
|
3.7
|
0.1
|
1.0
|
N
|
A:CYS167
|
3.7
|
0.4
|
1.0
|
CB
|
A:CYS167
|
3.9
|
0.7
|
1.0
|
CA
|
A:CYS110
|
4.0
|
0.5
|
1.0
|
CA
|
A:CYS167
|
4.2
|
0.1
|
1.0
|
C
|
A:CYS167
|
4.4
|
0.7
|
1.0
|
O
|
A:CYS167
|
4.5
|
0.7
|
1.0
|
C
|
A:GLY166
|
4.6
|
0.2
|
1.0
|
CA
|
A:CYS107
|
4.6
|
0.7
|
1.0
|
CA
|
A:CYS148
|
4.6
|
0.6
|
1.0
|
CA
|
A:GLY166
|
4.7
|
0.8
|
1.0
|
C
|
A:HIS109
|
4.7
|
0.8
|
1.0
|
C
|
A:CYS110
|
4.8
|
0.8
|
1.0
|
CB
|
A:HIS109
|
4.8
|
0.1
|
1.0
|
ND1
|
A:HIS109
|
4.9
|
0.0
|
1.0
|
N
|
A:GLY111
|
4.9
|
0.7
|
1.0
|
NE2
|
A:GLN171
|
5.0
|
0.6
|
1.0
|
|
Zinc binding site 2 out
of 8 in 5ip7
Go back to
Zinc Binding Sites List in 5ip7
Zinc binding site 2 out
of 8 in the Structure of Rna Polymerase II-TFG1 Peptide Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Structure of Rna Polymerase II-TFG1 Peptide Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1802
b:97.4
occ:1.00
|
NE2
|
A:HIS80
|
2.0
|
0.3
|
1.0
|
SG
|
A:CYS67
|
2.1
|
0.3
|
1.0
|
SG
|
A:CYS70
|
2.3
|
92.1
|
1.0
|
SG
|
A:CYS77
|
2.4
|
92.3
|
1.0
|
CD2
|
A:HIS80
|
3.0
|
0.6
|
1.0
|
CE1
|
A:HIS80
|
3.1
|
99.0
|
1.0
|
CB
|
A:CYS77
|
3.5
|
89.5
|
1.0
|
CB
|
A:CYS67
|
3.5
|
0.7
|
1.0
|
CB
|
A:CYS70
|
3.5
|
90.8
|
1.0
|
N
|
A:CYS70
|
3.8
|
95.7
|
1.0
|
CG
|
A:HIS80
|
4.1
|
98.3
|
1.0
|
ND1
|
A:HIS80
|
4.2
|
99.0
|
1.0
|
CA
|
A:CYS70
|
4.2
|
94.6
|
1.0
|
CB
|
A:THR69
|
4.3
|
0.1
|
1.0
|
CA
|
A:CYS77
|
4.5
|
88.1
|
1.0
|
O
|
A:CYS67
|
4.7
|
0.6
|
1.0
|
C
|
A:THR69
|
4.8
|
0.3
|
1.0
|
CA
|
A:CYS67
|
4.8
|
0.3
|
1.0
|
CG2
|
A:THR69
|
4.9
|
97.9
|
1.0
|
CD
|
A:PRO78
|
4.9
|
86.7
|
1.0
|
CA
|
A:THR69
|
4.9
|
0.1
|
1.0
|
CA
|
A:GLY59
|
4.9
|
98.5
|
1.0
|
N
|
A:GLY79
|
5.0
|
93.1
|
1.0
|
|
Zinc binding site 3 out
of 8 in 5ip7
Go back to
Zinc Binding Sites List in 5ip7
Zinc binding site 3 out
of 8 in the Structure of Rna Polymerase II-TFG1 Peptide Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Structure of Rna Polymerase II-TFG1 Peptide Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn1301
b:0.1
occ:1.00
|
SG
|
B:CYS1182
|
2.2
|
94.0
|
1.0
|
SG
|
B:CYS1166
|
2.2
|
98.3
|
1.0
|
SG
|
B:CYS1163
|
2.3
|
99.9
|
1.0
|
SG
|
B:CYS1185
|
2.4
|
0.1
|
1.0
|
CB
|
B:CYS1163
|
3.1
|
94.1
|
1.0
|
CB
|
B:CYS1166
|
3.1
|
95.4
|
1.0
|
CB
|
B:CYS1185
|
3.2
|
0.0
|
1.0
|
CB
|
B:CYS1182
|
3.5
|
91.6
|
1.0
|
N
|
B:CYS1166
|
3.7
|
95.5
|
1.0
|
CA
|
B:CYS1166
|
3.9
|
94.3
|
1.0
|
O
|
B:GLY1184
|
4.5
|
0.2
|
1.0
|
CA
|
B:CYS1163
|
4.6
|
92.4
|
1.0
|
CA
|
B:CYS1185
|
4.6
|
0.3
|
1.0
|
CB
|
B:ILE1165
|
4.6
|
0.2
|
1.0
|
C
|
B:CYS1166
|
4.7
|
95.5
|
1.0
|
C
|
B:ILE1165
|
4.9
|
99.8
|
1.0
|
CA
|
B:CYS1182
|
4.9
|
94.1
|
1.0
|
CD1
|
A:ILE30
|
4.9
|
0.5
|
1.0
|
O
|
B:CYS1182
|
4.9
|
0.6
|
1.0
|
CB
|
B:THR1170
|
4.9
|
0.4
|
1.0
|
N
|
B:GLY1167
|
5.0
|
90.5
|
1.0
|
|
Zinc binding site 4 out
of 8 in 5ip7
Go back to
Zinc Binding Sites List in 5ip7
Zinc binding site 4 out
of 8 in the Structure of Rna Polymerase II-TFG1 Peptide Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Structure of Rna Polymerase II-TFG1 Peptide Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn301
b:94.5
occ:1.00
|
SG
|
C:CYS88
|
2.2
|
93.2
|
1.0
|
SG
|
C:CYS92
|
2.2
|
0.5
|
1.0
|
SG
|
C:CYS86
|
2.3
|
83.5
|
1.0
|
SG
|
C:CYS95
|
2.3
|
92.8
|
1.0
|
CB
|
C:CYS92
|
3.1
|
0.3
|
1.0
|
N
|
C:CYS92
|
3.1
|
97.4
|
1.0
|
CB
|
C:CYS86
|
3.3
|
78.0
|
1.0
|
CB
|
C:CYS95
|
3.4
|
90.0
|
1.0
|
CB
|
C:CYS88
|
3.6
|
90.7
|
1.0
|
CA
|
C:CYS92
|
3.6
|
98.5
|
1.0
|
C
|
C:HIS91
|
3.8
|
0.5
|
1.0
|
N
|
C:CYS95
|
3.9
|
93.2
|
1.0
|
CA
|
C:HIS91
|
4.1
|
98.1
|
1.0
|
C
|
C:CYS92
|
4.2
|
0.4
|
1.0
|
CA
|
C:CYS95
|
4.2
|
91.7
|
1.0
|
N
|
C:CYS88
|
4.3
|
87.5
|
1.0
|
O
|
C:CYS92
|
4.4
|
98.6
|
1.0
|
CA
|
C:CYS88
|
4.6
|
89.7
|
1.0
|
O
|
C:HIS91
|
4.6
|
0.5
|
1.0
|
CA
|
C:CYS86
|
4.7
|
77.8
|
1.0
|
O
|
C:ASP90
|
4.7
|
0.4
|
1.0
|
CB
|
C:LYS94
|
4.8
|
94.1
|
1.0
|
N
|
C:LYS94
|
4.8
|
94.2
|
1.0
|
C
|
C:LYS94
|
4.9
|
97.8
|
1.0
|
N
|
C:PHE87
|
4.9
|
83.1
|
1.0
|
C
|
C:CYS86
|
5.0
|
83.8
|
1.0
|
N
|
C:ASP93
|
5.0
|
97.8
|
1.0
|
|
Zinc binding site 5 out
of 8 in 5ip7
Go back to
Zinc Binding Sites List in 5ip7
Zinc binding site 5 out
of 8 in the Structure of Rna Polymerase II-TFG1 Peptide Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of Structure of Rna Polymerase II-TFG1 Peptide Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:Zn201
b:0.8
occ:1.00
|
SG
|
I:CYS7
|
2.2
|
0.2
|
1.0
|
SG
|
I:CYS32
|
2.2
|
0.2
|
1.0
|
SG
|
I:CYS29
|
2.4
|
0.9
|
1.0
|
SG
|
I:CYS10
|
2.4
|
0.0
|
1.0
|
CB
|
I:CYS10
|
2.5
|
0.8
|
1.0
|
CB
|
I:CYS32
|
3.3
|
0.9
|
1.0
|
CB
|
I:CYS29
|
3.4
|
0.7
|
1.0
|
CB
|
I:CYS7
|
3.4
|
0.5
|
1.0
|
N
|
I:CYS32
|
3.9
|
0.8
|
1.0
|
CA
|
I:CYS10
|
3.9
|
0.6
|
1.0
|
O
|
I:ARG8
|
4.1
|
0.5
|
1.0
|
CA
|
I:CYS32
|
4.1
|
0.9
|
1.0
|
CB
|
I:TYR34
|
4.3
|
0.1
|
1.0
|
N
|
I:CYS10
|
4.3
|
0.6
|
1.0
|
C
|
I:THR31
|
4.5
|
0.7
|
1.0
|
CB
|
I:THR31
|
4.6
|
0.6
|
1.0
|
C
|
I:CYS32
|
4.7
|
0.3
|
1.0
|
C
|
I:ASP9
|
4.7
|
0.6
|
1.0
|
CA
|
I:CYS7
|
4.7
|
0.9
|
1.0
|
CA
|
I:CYS29
|
4.8
|
0.5
|
1.0
|
O
|
I:ASP9
|
4.9
|
0.7
|
1.0
|
C
|
I:CYS10
|
4.9
|
0.8
|
1.0
|
C
|
I:CYS7
|
4.9
|
0.6
|
1.0
|
O
|
I:CYS32
|
4.9
|
1.0
|
1.0
|
O
|
I:CYS7
|
4.9
|
0.3
|
1.0
|
CA
|
I:THR31
|
5.0
|
1.0
|
1.0
|
|
Zinc binding site 6 out
of 8 in 5ip7
Go back to
Zinc Binding Sites List in 5ip7
Zinc binding site 6 out
of 8 in the Structure of Rna Polymerase II-TFG1 Peptide Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 6 of Structure of Rna Polymerase II-TFG1 Peptide Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:Zn202
b:0.9
occ:1.00
|
SG
|
I:CYS78
|
2.2
|
0.2
|
1.0
|
SG
|
I:CYS106
|
2.3
|
0.6
|
1.0
|
SG
|
I:CYS75
|
2.3
|
0.6
|
1.0
|
SG
|
I:CYS103
|
2.4
|
0.3
|
1.0
|
CB
|
I:CYS75
|
3.0
|
0.9
|
1.0
|
CB
|
I:CYS103
|
3.0
|
0.7
|
1.0
|
CB
|
I:CYS106
|
3.1
|
0.5
|
1.0
|
CB
|
I:CYS78
|
3.4
|
0.5
|
1.0
|
N
|
I:CYS106
|
3.7
|
1.0
|
1.0
|
N
|
I:CYS78
|
3.7
|
0.2
|
1.0
|
CA
|
I:CYS106
|
3.9
|
0.9
|
1.0
|
CA
|
I:CYS78
|
4.1
|
0.4
|
1.0
|
CA
|
I:CYS75
|
4.5
|
0.7
|
1.0
|
CA
|
I:CYS103
|
4.5
|
0.4
|
1.0
|
CB
|
I:LYS77
|
4.6
|
0.0
|
1.0
|
N
|
I:SER107
|
4.6
|
0.5
|
1.0
|
C
|
I:CYS106
|
4.7
|
0.2
|
1.0
|
CB
|
I:SER105
|
4.7
|
0.5
|
1.0
|
N
|
I:HIS79
|
4.7
|
0.0
|
1.0
|
C
|
I:CYS78
|
4.8
|
0.7
|
1.0
|
C
|
I:LYS77
|
4.8
|
0.1
|
1.0
|
C
|
I:SER105
|
4.8
|
0.1
|
1.0
|
N
|
I:SER80
|
4.9
|
0.3
|
1.0
|
CB
|
I:SER80
|
4.9
|
1.0
|
1.0
|
|
Zinc binding site 7 out
of 8 in 5ip7
Go back to
Zinc Binding Sites List in 5ip7
Zinc binding site 7 out
of 8 in the Structure of Rna Polymerase II-TFG1 Peptide Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 7 of Structure of Rna Polymerase II-TFG1 Peptide Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
J:Zn101
b:0.0
occ:1.00
|
SG
|
J:CYS46
|
2.2
|
0.8
|
1.0
|
SG
|
J:CYS7
|
2.3
|
0.4
|
1.0
|
SG
|
J:CYS45
|
2.3
|
0.4
|
1.0
|
SG
|
J:CYS10
|
2.3
|
99.0
|
1.0
|
CB
|
J:CYS7
|
3.1
|
0.8
|
1.0
|
N
|
J:CYS46
|
3.3
|
0.1
|
1.0
|
CB
|
J:CYS45
|
3.5
|
98.0
|
1.0
|
CB
|
J:CYS10
|
3.5
|
94.5
|
1.0
|
CB
|
J:CYS46
|
3.6
|
0.7
|
1.0
|
CA
|
J:CYS46
|
3.7
|
0.7
|
1.0
|
C
|
J:CYS45
|
3.7
|
0.8
|
1.0
|
N
|
J:CYS10
|
3.8
|
90.4
|
1.0
|
CA
|
J:CYS10
|
4.1
|
92.3
|
1.0
|
CA
|
J:CYS45
|
4.2
|
98.9
|
1.0
|
O
|
J:CYS45
|
4.3
|
0.8
|
1.0
|
CG
|
J:ARG43
|
4.4
|
0.8
|
1.0
|
CA
|
J:CYS7
|
4.6
|
0.5
|
1.0
|
CB
|
J:SER9
|
4.7
|
92.1
|
1.0
|
C
|
J:CYS10
|
4.8
|
98.5
|
1.0
|
N
|
J:GLY11
|
4.8
|
95.8
|
1.0
|
CB
|
J:LYS12
|
4.8
|
0.8
|
1.0
|
C
|
J:SER9
|
4.9
|
92.1
|
1.0
|
N
|
J:CYS45
|
4.9
|
0.1
|
1.0
|
CZ
|
J:ARG43
|
4.9
|
0.3
|
1.0
|
N
|
J:LYS12
|
4.9
|
0.3
|
1.0
|
|
Zinc binding site 8 out
of 8 in 5ip7
Go back to
Zinc Binding Sites List in 5ip7
Zinc binding site 8 out
of 8 in the Structure of Rna Polymerase II-TFG1 Peptide Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 8 of Structure of Rna Polymerase II-TFG1 Peptide Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
L:Zn101
b:0.4
occ:1.00
|
SG
|
L:CYS34
|
2.3
|
1.0
|
1.0
|
SG
|
L:CYS48
|
2.3
|
0.3
|
1.0
|
SG
|
L:CYS51
|
2.3
|
0.8
|
1.0
|
SG
|
L:CYS31
|
2.4
|
0.6
|
1.0
|
CB
|
L:CYS34
|
3.2
|
0.4
|
1.0
|
CB
|
L:CYS48
|
3.2
|
0.9
|
1.0
|
CB
|
L:CYS31
|
3.3
|
0.6
|
1.0
|
O
|
L:CYS51
|
3.6
|
0.1
|
1.0
|
N
|
L:CYS34
|
3.8
|
0.6
|
1.0
|
CB
|
L:CYS51
|
4.0
|
0.2
|
1.0
|
CA
|
L:CYS34
|
4.1
|
0.3
|
1.0
|
N
|
L:CYS51
|
4.1
|
0.6
|
1.0
|
CB
|
L:HIS53
|
4.4
|
0.1
|
1.0
|
C
|
L:CYS51
|
4.4
|
0.5
|
1.0
|
CA
|
L:CYS51
|
4.4
|
0.0
|
1.0
|
CA
|
L:CYS48
|
4.6
|
0.5
|
1.0
|
CB
|
L:ASP50
|
4.7
|
0.5
|
1.0
|
N
|
L:SER35
|
4.7
|
0.1
|
1.0
|
C
|
L:CYS34
|
4.7
|
0.8
|
1.0
|
CA
|
L:CYS31
|
4.7
|
0.5
|
1.0
|
|
Reference:
C.Plaschka,
M.Hantsche,
C.Dienemann,
C.Burzinski,
J.Plitzko,
P.Cramer.
Transcription Initiation Complex Structures Elucidate Dna Opening. Nature V. 533 353 2016.
ISSN: ESSN 1476-4687
PubMed: 27193681
DOI: 10.1038/NATURE17990
Page generated: Sun Oct 27 18:18:34 2024
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