Zinc in PDB 3g8q: A Cytidine Deaminase Edits C-to-U in Transfer Rnas in Archaea
Protein crystallography data
The structure of A Cytidine Deaminase Edits C-to-U in Transfer Rnas in Archaea, PDB code: 3g8q
was solved by
Y.Xiong,
B.J.Stanley,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
30.00 /
2.40
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
184.465,
77.060,
109.082,
90.00,
103.57,
90.00
|
R / Rfree (%)
|
20.2 /
26.5
|
Other elements in 3g8q:
The structure of A Cytidine Deaminase Edits C-to-U in Transfer Rnas in Archaea also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the A Cytidine Deaminase Edits C-to-U in Transfer Rnas in Archaea
(pdb code 3g8q). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
A Cytidine Deaminase Edits C-to-U in Transfer Rnas in Archaea, PDB code: 3g8q:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 3g8q
Go back to
Zinc Binding Sites List in 3g8q
Zinc binding site 1 out
of 4 in the A Cytidine Deaminase Edits C-to-U in Transfer Rnas in Archaea
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of A Cytidine Deaminase Edits C-to-U in Transfer Rnas in Archaea within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn301
b:0.4
occ:1.00
|
SG
|
A:CYS70
|
2.3
|
67.8
|
1.0
|
ND1
|
A:HIS44
|
2.7
|
70.8
|
1.0
|
SG
|
A:CYS67
|
2.8
|
56.4
|
1.0
|
O
|
A:HOH326
|
2.9
|
40.2
|
1.0
|
CG
|
A:HIS44
|
3.0
|
66.6
|
1.0
|
CE1
|
A:HIS44
|
3.3
|
68.8
|
1.0
|
CB
|
A:CYS70
|
3.4
|
59.2
|
1.0
|
CB
|
A:HIS44
|
3.4
|
61.3
|
1.0
|
N
|
A:CYS67
|
3.6
|
40.2
|
1.0
|
OE2
|
A:GLU46
|
3.6
|
59.2
|
1.0
|
CB
|
A:CYS67
|
3.6
|
47.1
|
1.0
|
CD2
|
A:HIS44
|
3.7
|
69.2
|
1.0
|
OE1
|
A:GLU46
|
3.9
|
54.0
|
1.0
|
NE2
|
A:HIS44
|
3.9
|
69.8
|
1.0
|
CD
|
A:GLU46
|
3.9
|
52.4
|
1.0
|
CA
|
A:CYS67
|
4.2
|
42.5
|
1.0
|
CA
|
A:CYS70
|
4.6
|
60.0
|
1.0
|
C
|
A:PRO66
|
4.6
|
38.7
|
1.0
|
N
|
A:CYS70
|
4.6
|
60.5
|
1.0
|
CA
|
A:PRO66
|
4.7
|
40.7
|
1.0
|
O
|
A:CYS67
|
4.8
|
43.3
|
1.0
|
C
|
A:CYS67
|
4.8
|
45.1
|
1.0
|
CA
|
A:HIS44
|
4.8
|
62.0
|
1.0
|
|
Zinc binding site 2 out
of 4 in 3g8q
Go back to
Zinc Binding Sites List in 3g8q
Zinc binding site 2 out
of 4 in the A Cytidine Deaminase Edits C-to-U in Transfer Rnas in Archaea
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of A Cytidine Deaminase Edits C-to-U in Transfer Rnas in Archaea within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn301
b:0.5
occ:1.00
|
SG
|
B:CYS70
|
2.2
|
67.6
|
1.0
|
ND1
|
B:HIS44
|
2.4
|
75.5
|
1.0
|
SG
|
B:CYS67
|
2.8
|
65.0
|
1.0
|
CG
|
B:HIS44
|
3.0
|
75.0
|
1.0
|
CE1
|
B:HIS44
|
3.1
|
78.1
|
1.0
|
CB
|
B:CYS67
|
3.2
|
62.6
|
1.0
|
CB
|
B:HIS44
|
3.4
|
70.4
|
1.0
|
O
|
B:HOH305
|
3.5
|
57.4
|
1.0
|
N
|
B:CYS67
|
3.5
|
58.9
|
1.0
|
CB
|
B:CYS70
|
3.5
|
61.9
|
1.0
|
OE2
|
B:GLU46
|
3.7
|
56.1
|
1.0
|
CA
|
B:CYS67
|
3.9
|
59.9
|
1.0
|
CD2
|
B:HIS44
|
3.9
|
81.8
|
1.0
|
NE2
|
B:HIS44
|
4.0
|
81.3
|
1.0
|
OE1
|
B:GLU46
|
4.1
|
67.1
|
1.0
|
CD
|
B:GLU46
|
4.2
|
59.4
|
1.0
|
N
|
B:CYS70
|
4.5
|
62.5
|
1.0
|
C
|
B:PRO66
|
4.5
|
57.0
|
1.0
|
CA
|
B:CYS70
|
4.6
|
62.8
|
1.0
|
C
|
B:CYS67
|
4.6
|
59.0
|
1.0
|
O
|
B:CYS67
|
4.7
|
57.9
|
1.0
|
CA
|
B:PRO66
|
4.8
|
53.9
|
1.0
|
CA
|
B:HIS44
|
4.9
|
70.4
|
1.0
|
|
Zinc binding site 3 out
of 4 in 3g8q
Go back to
Zinc Binding Sites List in 3g8q
Zinc binding site 3 out
of 4 in the A Cytidine Deaminase Edits C-to-U in Transfer Rnas in Archaea
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of A Cytidine Deaminase Edits C-to-U in Transfer Rnas in Archaea within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn301
b:0.1
occ:1.00
|
SG
|
C:CYS70
|
2.5
|
65.2
|
1.0
|
CG
|
C:HIS44
|
2.6
|
68.9
|
1.0
|
ND1
|
C:HIS44
|
2.7
|
73.2
|
1.0
|
SG
|
C:CYS67
|
2.8
|
64.1
|
1.0
|
CD2
|
C:HIS44
|
3.0
|
67.3
|
1.0
|
CB
|
C:HIS44
|
3.1
|
65.7
|
1.0
|
O
|
C:HOH304
|
3.1
|
49.8
|
1.0
|
CE1
|
C:HIS44
|
3.1
|
72.5
|
1.0
|
NE2
|
C:HIS44
|
3.3
|
68.8
|
1.0
|
CB
|
C:CYS67
|
3.4
|
55.4
|
1.0
|
CB
|
C:CYS70
|
3.6
|
60.0
|
1.0
|
OE1
|
C:GLU46
|
3.7
|
62.1
|
1.0
|
N
|
C:CYS67
|
3.9
|
52.0
|
1.0
|
OE2
|
C:GLU46
|
4.1
|
65.8
|
1.0
|
CD
|
C:GLU46
|
4.2
|
63.7
|
1.0
|
CA
|
C:CYS67
|
4.3
|
54.1
|
1.0
|
NE
|
C:ARG47
|
4.5
|
0.7
|
1.0
|
N
|
C:CYS70
|
4.5
|
63.4
|
1.0
|
CA
|
C:HIS44
|
4.5
|
66.2
|
1.0
|
CA
|
C:CYS70
|
4.7
|
62.9
|
1.0
|
NH2
|
C:ARG47
|
4.7
|
0.5
|
1.0
|
CZ
|
C:ARG47
|
4.8
|
0.5
|
1.0
|
O
|
C:CYS67
|
4.9
|
52.4
|
1.0
|
C
|
C:CYS67
|
4.9
|
55.5
|
1.0
|
|
Zinc binding site 4 out
of 4 in 3g8q
Go back to
Zinc Binding Sites List in 3g8q
Zinc binding site 4 out
of 4 in the A Cytidine Deaminase Edits C-to-U in Transfer Rnas in Archaea
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of A Cytidine Deaminase Edits C-to-U in Transfer Rnas in Archaea within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn301
b:88.7
occ:1.00
|
SG
|
D:CYS70
|
2.4
|
55.3
|
1.0
|
SG
|
D:CYS67
|
2.5
|
49.8
|
1.0
|
ND1
|
D:HIS44
|
2.9
|
58.6
|
1.0
|
O
|
D:HOH305
|
3.0
|
39.2
|
1.0
|
CB
|
D:CYS70
|
3.1
|
42.4
|
1.0
|
CG
|
D:HIS44
|
3.2
|
54.1
|
1.0
|
CB
|
D:CYS67
|
3.2
|
40.5
|
1.0
|
CE1
|
D:HIS44
|
3.4
|
55.1
|
1.0
|
N
|
D:CYS67
|
3.5
|
41.1
|
1.0
|
CB
|
D:HIS44
|
3.6
|
53.1
|
1.0
|
CD2
|
D:HIS44
|
3.7
|
55.0
|
1.0
|
CA
|
D:CYS67
|
3.8
|
40.2
|
1.0
|
NE2
|
D:HIS44
|
3.9
|
58.5
|
1.0
|
OE1
|
D:GLU46
|
4.1
|
49.6
|
1.0
|
OE2
|
D:GLU46
|
4.1
|
49.7
|
1.0
|
N
|
D:CYS70
|
4.2
|
40.1
|
1.0
|
CD
|
D:GLU46
|
4.2
|
46.5
|
1.0
|
CA
|
D:CYS70
|
4.2
|
41.2
|
1.0
|
O
|
D:CYS67
|
4.3
|
39.2
|
1.0
|
C
|
D:CYS67
|
4.4
|
40.3
|
1.0
|
C
|
D:PRO66
|
4.6
|
38.4
|
1.0
|
O
|
D:HOH314
|
4.8
|
72.8
|
1.0
|
CA
|
D:PRO66
|
4.8
|
37.7
|
1.0
|
|
Reference:
L.Randau,
B.J.Stanley,
A.Kohlway,
S.Mechta,
Y.Xiong,
D.Soll.
A Cytidine Deaminase Edits C to U in Transfer Rnas in Archaea Science V. 324 657 2009.
ISSN: ISSN 0036-8075
PubMed: 19407206
DOI: 10.1126/SCIENCE.1170123
Page generated: Thu Oct 24 13:35:49 2024
|