Zinc in PDB 4y52: Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation.
Enzymatic activity of Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation.
All present enzymatic activity of Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation.:
2.7.7.6;
Protein crystallography data
The structure of Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation., PDB code: 4y52
was solved by
L.Wang,
J.Chong,
D.Wang,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
49.27 /
3.50
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
166.703,
221.644,
192.410,
90.00,
100.35,
90.00
|
R / Rfree (%)
|
20.1 /
23.2
|
Other elements in 4y52:
The structure of Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation. also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation.
(pdb code 4y52). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 8 binding sites of Zinc where determined in the
Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation., PDB code: 4y52:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Zinc binding site 1 out
of 8 in 4y52
Go back to
Zinc Binding Sites List in 4y52
Zinc binding site 1 out
of 8 in the Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1801
b:0.7
occ:1.00
|
SG
|
A:CYS167
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS110
|
2.4
|
0.5
|
1.0
|
SG
|
A:CYS148
|
2.4
|
0.0
|
1.0
|
SG
|
A:CYS107
|
2.4
|
0.5
|
1.0
|
CB
|
A:CYS107
|
2.6
|
0.3
|
1.0
|
CB
|
A:CYS110
|
4.0
|
0.0
|
1.0
|
CB
|
A:CYS167
|
4.0
|
0.2
|
1.0
|
O
|
A:CYS167
|
4.0
|
0.8
|
1.0
|
CB
|
A:CYS148
|
4.1
|
0.3
|
1.0
|
CA
|
A:CYS107
|
4.2
|
0.9
|
1.0
|
N
|
A:CYS110
|
4.3
|
0.2
|
1.0
|
C
|
A:CYS167
|
4.5
|
0.1
|
1.0
|
CA
|
A:CYS167
|
4.6
|
0.3
|
1.0
|
CA
|
A:CYS110
|
4.7
|
0.2
|
1.0
|
N
|
A:CYS167
|
4.7
|
0.2
|
1.0
|
C
|
A:CYS107
|
4.8
|
0.4
|
1.0
|
N
|
A:CYS107
|
4.9
|
0.9
|
1.0
|
CB
|
A:HIS109
|
4.9
|
0.4
|
1.0
|
|
Zinc binding site 2 out
of 8 in 4y52
Go back to
Zinc Binding Sites List in 4y52
Zinc binding site 2 out
of 8 in the Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1802
b:0.9
occ:1.00
|
SG
|
A:CYS67
|
2.2
|
0.1
|
1.0
|
NE2
|
A:HIS80
|
2.2
|
0.1
|
1.0
|
SG
|
A:CYS77
|
2.3
|
0.1
|
1.0
|
CE1
|
A:HIS80
|
2.4
|
0.7
|
1.0
|
SG
|
A:CYS70
|
2.4
|
0.3
|
1.0
|
CB
|
A:CYS77
|
3.1
|
0.8
|
1.0
|
O
|
A:CYS67
|
3.3
|
0.7
|
1.0
|
CB
|
A:CYS67
|
3.4
|
0.3
|
1.0
|
CD2
|
A:HIS80
|
3.6
|
0.9
|
1.0
|
CB
|
A:CYS70
|
3.7
|
0.4
|
1.0
|
ND1
|
A:HIS80
|
3.7
|
90.7
|
1.0
|
C
|
A:CYS67
|
3.8
|
0.3
|
1.0
|
CA
|
A:CYS67
|
4.2
|
0.4
|
1.0
|
CG
|
A:HIS80
|
4.3
|
0.7
|
1.0
|
CB
|
A:GLN68
|
4.4
|
0.7
|
1.0
|
CA
|
A:CYS77
|
4.5
|
0.6
|
1.0
|
N
|
A:GLN68
|
4.7
|
0.1
|
1.0
|
O
|
A:GLN71
|
4.8
|
0.6
|
1.0
|
CA
|
A:CYS70
|
4.9
|
0.7
|
1.0
|
|
Zinc binding site 3 out
of 8 in 4y52
Go back to
Zinc Binding Sites List in 4y52
Zinc binding site 3 out
of 8 in the Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn1301
b:1.0
occ:1.00
|
SG
|
B:CYS1166
|
2.3
|
78.4
|
1.0
|
SG
|
B:CYS1163
|
2.3
|
0.7
|
1.0
|
SG
|
B:CYS1185
|
2.3
|
0.8
|
1.0
|
SG
|
B:CYS1182
|
2.4
|
0.4
|
1.0
|
CB
|
B:CYS1163
|
3.1
|
0.7
|
1.0
|
CB
|
B:CYS1185
|
3.4
|
0.7
|
1.0
|
CB
|
B:CYS1166
|
3.6
|
96.9
|
1.0
|
N
|
B:CYS1166
|
3.8
|
0.4
|
1.0
|
CB
|
B:CYS1182
|
4.0
|
0.0
|
1.0
|
CB
|
B:ILE1165
|
4.2
|
0.1
|
1.0
|
O
|
B:CYS1182
|
4.3
|
0.6
|
1.0
|
CA
|
B:CYS1166
|
4.4
|
0.2
|
1.0
|
N
|
B:CYS1185
|
4.5
|
0.6
|
1.0
|
CA
|
B:CYS1185
|
4.6
|
0.7
|
1.0
|
CA
|
B:CYS1163
|
4.6
|
0.3
|
1.0
|
CG1
|
B:ILE1165
|
4.8
|
0.3
|
1.0
|
C
|
B:ILE1165
|
4.9
|
0.3
|
1.0
|
CA
|
B:ILE1165
|
5.0
|
0.2
|
1.0
|
|
Zinc binding site 4 out
of 8 in 4y52
Go back to
Zinc Binding Sites List in 4y52
Zinc binding site 4 out
of 8 in the Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn401
b:96.1
occ:1.00
|
SG
|
C:CYS86
|
2.2
|
62.8
|
1.0
|
SG
|
C:CYS92
|
2.2
|
49.8
|
1.0
|
SG
|
C:CYS95
|
2.2
|
79.5
|
1.0
|
SG
|
C:CYS88
|
2.3
|
53.1
|
1.0
|
CB
|
C:CYS86
|
2.9
|
76.2
|
1.0
|
CB
|
C:CYS92
|
3.2
|
54.4
|
1.0
|
N
|
C:CYS92
|
3.4
|
93.6
|
1.0
|
CB
|
C:CYS95
|
3.5
|
86.9
|
1.0
|
C
|
C:HIS91
|
3.8
|
0.9
|
1.0
|
CA
|
C:CYS92
|
3.8
|
73.7
|
1.0
|
CB
|
C:CYS88
|
3.9
|
0.0
|
1.0
|
CA
|
C:HIS91
|
4.1
|
87.8
|
1.0
|
O
|
C:ASP90
|
4.2
|
75.7
|
1.0
|
CA
|
C:CYS86
|
4.4
|
67.3
|
1.0
|
N
|
C:CYS95
|
4.4
|
94.7
|
1.0
|
CA
|
C:CYS95
|
4.5
|
71.9
|
1.0
|
O
|
C:HIS91
|
4.5
|
93.4
|
1.0
|
C
|
C:CYS92
|
4.6
|
73.0
|
1.0
|
N
|
C:CYS88
|
4.7
|
67.8
|
1.0
|
CA
|
C:CYS88
|
4.8
|
87.3
|
1.0
|
O
|
C:CYS88
|
4.9
|
83.7
|
1.0
|
O
|
C:CYS92
|
4.9
|
75.8
|
1.0
|
C
|
C:CYS95
|
4.9
|
47.5
|
1.0
|
C
|
C:CYS86
|
4.9
|
77.9
|
1.0
|
CA
|
C:SER83
|
5.0
|
45.5
|
1.0
|
|
Zinc binding site 5 out
of 8 in 4y52
Go back to
Zinc Binding Sites List in 4y52
Zinc binding site 5 out
of 8 in the Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:Zn201
b:0.4
occ:1.00
|
SG
|
I:CYS10
|
2.3
|
65.1
|
1.0
|
SG
|
I:CYS29
|
2.3
|
0.4
|
1.0
|
SG
|
I:CYS32
|
2.4
|
77.1
|
1.0
|
SG
|
I:CYS7
|
2.4
|
74.6
|
1.0
|
CB
|
I:CYS29
|
3.1
|
68.1
|
1.0
|
CB
|
I:CYS7
|
3.1
|
63.8
|
1.0
|
CB
|
I:CYS32
|
3.6
|
95.4
|
1.0
|
CB
|
I:CYS10
|
3.7
|
88.2
|
1.0
|
N
|
I:CYS32
|
3.8
|
91.4
|
1.0
|
CB
|
I:THR31
|
4.1
|
85.6
|
1.0
|
CB
|
I:TYR34
|
4.1
|
48.4
|
1.0
|
CA
|
I:CYS32
|
4.3
|
0.1
|
1.0
|
N
|
I:CYS10
|
4.3
|
0.7
|
1.0
|
C
|
I:THR31
|
4.4
|
1.0
|
1.0
|
CA
|
I:CYS29
|
4.5
|
70.4
|
1.0
|
N
|
I:TYR34
|
4.5
|
55.7
|
1.0
|
CA
|
I:CYS7
|
4.6
|
81.0
|
1.0
|
N
|
I:SER33
|
4.6
|
0.9
|
1.0
|
CA
|
I:CYS10
|
4.6
|
0.0
|
1.0
|
CA
|
I:THR31
|
4.6
|
73.9
|
1.0
|
N
|
I:THR31
|
4.6
|
94.3
|
1.0
|
OG1
|
I:THR31
|
4.7
|
0.9
|
1.0
|
CB
|
I:ASP9
|
4.8
|
0.7
|
1.0
|
C
|
I:CYS29
|
4.9
|
0.1
|
1.0
|
C
|
I:CYS32
|
4.9
|
0.4
|
1.0
|
CA
|
I:TYR34
|
5.0
|
59.0
|
1.0
|
|
Zinc binding site 6 out
of 8 in 4y52
Go back to
Zinc Binding Sites List in 4y52
Zinc binding site 6 out
of 8 in the Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 6 of Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:Zn202
b:96.1
occ:1.00
|
SG
|
I:CYS78
|
2.2
|
73.7
|
1.0
|
SG
|
I:CYS103
|
2.3
|
91.2
|
1.0
|
SG
|
I:CYS106
|
2.3
|
40.8
|
1.0
|
SG
|
I:CYS75
|
2.4
|
94.4
|
1.0
|
CB
|
I:CYS103
|
2.7
|
66.9
|
1.0
|
CB
|
I:CYS75
|
3.0
|
81.1
|
1.0
|
CB
|
I:CYS106
|
3.6
|
22.1
|
1.0
|
CB
|
I:CYS78
|
3.6
|
56.3
|
1.0
|
N
|
I:CYS78
|
3.7
|
61.5
|
1.0
|
N
|
I:CYS106
|
3.9
|
80.7
|
1.0
|
CA
|
I:CYS103
|
4.1
|
56.1
|
1.0
|
CA
|
I:CYS78
|
4.1
|
23.9
|
1.0
|
CB
|
I:LYS77
|
4.2
|
0.1
|
1.0
|
CA
|
I:CYS106
|
4.3
|
42.4
|
1.0
|
CB
|
I:HIS108
|
4.4
|
81.0
|
1.0
|
CA
|
I:CYS75
|
4.5
|
59.4
|
1.0
|
CB
|
I:SER80
|
4.6
|
36.9
|
1.0
|
C
|
I:CYS78
|
4.7
|
65.0
|
1.0
|
C
|
I:LYS77
|
4.7
|
79.7
|
1.0
|
CD2
|
I:HIS108
|
4.8
|
84.7
|
1.0
|
N
|
I:HIS108
|
4.8
|
70.3
|
1.0
|
CA
|
I:LYS77
|
4.9
|
60.4
|
1.0
|
N
|
I:HIS79
|
4.9
|
85.7
|
1.0
|
C
|
I:CYS106
|
4.9
|
48.7
|
1.0
|
N
|
I:LYS77
|
4.9
|
87.9
|
1.0
|
C
|
I:CYS103
|
4.9
|
70.7
|
1.0
|
N
|
I:SER107
|
4.9
|
1.0
|
1.0
|
N
|
I:SER80
|
5.0
|
43.2
|
1.0
|
CG
|
I:HIS108
|
5.0
|
90.0
|
1.0
|
N
|
I:CYS103
|
5.0
|
58.5
|
1.0
|
|
Zinc binding site 7 out
of 8 in 4y52
Go back to
Zinc Binding Sites List in 4y52
Zinc binding site 7 out
of 8 in the Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 7 of Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
J:Zn101
b:76.2
occ:1.00
|
SG
|
J:CYS46
|
2.3
|
48.6
|
1.0
|
SG
|
J:CYS10
|
2.3
|
62.7
|
1.0
|
SG
|
J:CYS7
|
2.3
|
36.9
|
1.0
|
SG
|
J:CYS45
|
2.3
|
72.2
|
1.0
|
CB
|
J:CYS46
|
2.9
|
32.4
|
1.0
|
N
|
J:CYS46
|
2.9
|
37.9
|
1.0
|
CA
|
J:CYS46
|
3.2
|
43.3
|
1.0
|
N
|
J:CYS10
|
3.4
|
54.8
|
1.0
|
CB
|
J:SER9
|
3.5
|
70.1
|
1.0
|
CB
|
J:CYS7
|
3.6
|
52.8
|
1.0
|
CB
|
J:CYS45
|
3.6
|
61.9
|
1.0
|
CB
|
J:CYS10
|
3.7
|
70.2
|
1.0
|
C
|
J:CYS45
|
3.8
|
57.8
|
1.0
|
CD
|
J:ARG43
|
4.1
|
86.5
|
1.0
|
CA
|
J:CYS10
|
4.1
|
69.3
|
1.0
|
CA
|
J:CYS45
|
4.3
|
47.5
|
1.0
|
N
|
J:GLY11
|
4.3
|
81.8
|
1.0
|
CG
|
J:ARG43
|
4.3
|
78.5
|
1.0
|
C
|
J:SER9
|
4.3
|
57.1
|
1.0
|
CA
|
J:SER9
|
4.3
|
59.0
|
1.0
|
NE
|
J:ARG43
|
4.4
|
50.9
|
1.0
|
OG
|
J:SER9
|
4.5
|
69.3
|
1.0
|
O
|
J:CYS45
|
4.6
|
61.5
|
1.0
|
N
|
J:SER9
|
4.6
|
65.9
|
1.0
|
C
|
J:CYS46
|
4.7
|
40.2
|
1.0
|
C
|
J:CYS10
|
4.7
|
57.5
|
1.0
|
CB
|
J:LYS12
|
4.7
|
72.3
|
1.0
|
N
|
J:LYS12
|
4.7
|
66.8
|
1.0
|
CA
|
J:CYS7
|
4.9
|
51.3
|
1.0
|
N
|
J:CYS45
|
5.0
|
50.1
|
1.0
|
|
Zinc binding site 8 out
of 8 in 4y52
Go back to
Zinc Binding Sites List in 4y52
Zinc binding site 8 out
of 8 in the Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 8 of Crystal Structure of 5-Carboxycytosine Recognition By Rna Polymerase II During Transcription Elongation. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
L:Zn101
b:0.2
occ:1.00
|
SG
|
L:CYS31
|
2.3
|
0.3
|
1.0
|
SG
|
L:CYS51
|
2.3
|
0.5
|
1.0
|
SG
|
L:CYS48
|
2.4
|
0.8
|
1.0
|
SG
|
L:CYS34
|
2.4
|
0.6
|
1.0
|
CB
|
L:CYS34
|
2.7
|
0.3
|
1.0
|
CB
|
L:CYS51
|
2.8
|
0.8
|
1.0
|
CB
|
L:CYS31
|
2.9
|
0.4
|
1.0
|
CB
|
L:CYS48
|
3.7
|
0.3
|
1.0
|
O
|
L:LYS49
|
3.8
|
0.5
|
1.0
|
CA
|
L:CYS51
|
4.0
|
0.7
|
1.0
|
CA
|
L:CYS34
|
4.0
|
0.5
|
1.0
|
N
|
L:CYS51
|
4.2
|
0.2
|
1.0
|
C
|
L:CYS34
|
4.3
|
0.5
|
1.0
|
CA
|
L:CYS31
|
4.4
|
0.8
|
1.0
|
OG
|
L:SER36
|
4.5
|
77.0
|
1.0
|
N
|
L:LYS49
|
4.5
|
0.0
|
1.0
|
N
|
L:CYS34
|
4.6
|
0.8
|
1.0
|
O
|
L:CYS34
|
4.7
|
0.7
|
1.0
|
C
|
L:LYS49
|
4.7
|
0.3
|
1.0
|
CB
|
L:SER36
|
4.8
|
0.0
|
1.0
|
N
|
L:SER35
|
4.8
|
0.0
|
1.0
|
|
Reference:
L.Wang,
Y.Zhou,
L.Xu,
R.Xiao,
X.Lu,
L.Chen,
J.Chong,
H.Li,
C.He,
X.D.Fu,
D.Wang.
Molecular Basis For 5-Carboxycytosine Recognition By Rna Polymerase II Elongation Complex. Nature V. 523 621 2015.
ISSN: ESSN 1476-4687
PubMed: 26123024
DOI: 10.1038/NATURE14482
Page generated: Sun Oct 27 10:55:43 2024
|