Mercury in PDB 4bjj: SFC1-SFC7 Dimerization Module
Protein crystallography data
The structure of SFC1-SFC7 Dimerization Module, PDB code: 4bjj
was solved by
N.M.I.Taylor,
F.Baudin,
G.Von Scheven,
C.W.Muller,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
33.290 /
2.40
|
Space group
|
P 63 2 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
85.245,
85.245,
154.108,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
18.09 /
22.36
|
Mercury Binding Sites:
The binding sites of Mercury atom in the SFC1-SFC7 Dimerization Module
(pdb code 4bjj). This binding sites where shown within
5.0 Angstroms radius around Mercury atom.
In total 3 binding sites of Mercury where determined in the
SFC1-SFC7 Dimerization Module, PDB code: 4bjj:
Jump to Mercury binding site number:
1;
2;
3;
Mercury binding site 1 out
of 3 in 4bjj
Go back to
Mercury Binding Sites List in 4bjj
Mercury binding site 1 out
of 3 in the SFC1-SFC7 Dimerization Module
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 1 of SFC1-SFC7 Dimerization Module within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Hg1109
b:53.2
occ:1.00
|
SG
|
A:CYS40
|
2.2
|
52.6
|
1.0
|
HA
|
B:SER70
|
2.9
|
57.5
|
1.0
|
HA
|
A:GLN41
|
3.0
|
43.5
|
1.0
|
O
|
B:PRO69
|
3.1
|
34.4
|
1.0
|
HB3
|
A:CYS40
|
3.3
|
55.0
|
1.0
|
CB
|
A:CYS40
|
3.4
|
45.8
|
1.0
|
HD2
|
A:PHE44
|
3.4
|
58.7
|
1.0
|
C
|
A:CYS40
|
3.4
|
41.2
|
1.0
|
N
|
A:GLN41
|
3.4
|
35.4
|
1.0
|
O
|
A:CYS40
|
3.5
|
41.6
|
1.0
|
CA
|
A:GLN41
|
3.7
|
36.3
|
1.0
|
H
|
A:GLN41
|
3.7
|
42.5
|
1.0
|
CA
|
B:SER70
|
3.8
|
48.0
|
1.0
|
C
|
B:PRO69
|
3.8
|
36.5
|
1.0
|
HG13
|
B:VAL68
|
3.9
|
55.9
|
1.0
|
CD2
|
A:PHE44
|
3.9
|
48.9
|
1.0
|
HB2
|
A:GLN41
|
3.9
|
51.7
|
1.0
|
N
|
B:SER70
|
4.0
|
43.1
|
1.0
|
CA
|
A:CYS40
|
4.0
|
42.6
|
1.0
|
HE2
|
A:PHE44
|
4.0
|
54.4
|
1.0
|
HB2
|
A:CYS40
|
4.2
|
55.0
|
1.0
|
CE2
|
A:PHE44
|
4.3
|
45.4
|
1.0
|
CB
|
A:GLN41
|
4.4
|
43.1
|
1.0
|
HB2
|
B:SER70
|
4.4
|
54.4
|
1.0
|
HB2
|
A:PHE44
|
4.5
|
53.8
|
1.0
|
HA
|
A:CYS40
|
4.5
|
51.1
|
1.0
|
HG12
|
B:VAL68
|
4.5
|
55.9
|
1.0
|
H
|
B:SER70
|
4.6
|
51.7
|
1.0
|
CG1
|
B:VAL68
|
4.7
|
46.6
|
1.0
|
O
|
A:GLN37
|
4.7
|
49.4
|
1.0
|
CB
|
B:SER70
|
4.7
|
45.3
|
1.0
|
C
|
B:SER70
|
4.8
|
60.1
|
1.0
|
CG
|
A:PHE44
|
4.9
|
50.6
|
1.0
|
HB3
|
A:GLN41
|
4.9
|
51.7
|
1.0
|
C
|
A:GLN41
|
5.0
|
45.4
|
1.0
|
HB
|
B:VAL68
|
5.0
|
47.4
|
1.0
|
|
Mercury binding site 2 out
of 3 in 4bjj
Go back to
Mercury Binding Sites List in 4bjj
Mercury binding site 2 out
of 3 in the SFC1-SFC7 Dimerization Module
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 2 of SFC1-SFC7 Dimerization Module within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Hg1101
b:0.3
occ:0.61
|
SG
|
B:CYS84
|
2.0
|
89.1
|
0.7
|
HB2
|
B:CYS84
|
2.4
|
80.0
|
0.3
|
HB2
|
B:CYS84
|
2.6
|
81.3
|
0.7
|
HB3
|
B:CYS84
|
2.6
|
80.0
|
0.3
|
CB
|
B:CYS84
|
2.8
|
67.7
|
0.7
|
CB
|
B:CYS84
|
2.9
|
66.6
|
0.3
|
O
|
B:CYS84
|
3.0
|
81.8
|
1.0
|
C
|
B:CYS84
|
3.3
|
69.6
|
1.0
|
HB3
|
B:CYS84
|
3.6
|
81.3
|
0.7
|
CA
|
B:CYS84
|
3.6
|
65.7
|
0.7
|
CA
|
B:CYS84
|
3.7
|
66.1
|
0.3
|
HA
|
B:LYS85
|
3.7
|
73.3
|
1.0
|
N
|
B:LYS85
|
4.0
|
61.8
|
1.0
|
HG3
|
B:LYS85
|
4.1
|
96.5
|
1.0
|
HG2
|
B:LYS85
|
4.1
|
96.5
|
1.0
|
HA
|
B:CYS84
|
4.1
|
78.9
|
0.7
|
HA
|
B:CYS84
|
4.2
|
79.3
|
0.3
|
SG
|
B:CYS84
|
4.3
|
63.1
|
0.3
|
CA
|
B:LYS85
|
4.4
|
61.1
|
1.0
|
CG
|
B:LYS85
|
4.5
|
80.4
|
1.0
|
H
|
B:LYS85
|
4.5
|
74.2
|
1.0
|
HE22
|
B:GLN60
|
4.6
|
79.3
|
1.0
|
H
|
B:CYS84
|
4.7
|
81.6
|
0.3
|
H
|
B:CYS84
|
4.7
|
81.6
|
0.7
|
N
|
B:CYS84
|
4.8
|
68.0
|
1.0
|
|
Mercury binding site 3 out
of 3 in 4bjj
Go back to
Mercury Binding Sites List in 4bjj
Mercury binding site 3 out
of 3 in the SFC1-SFC7 Dimerization Module
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 3 of SFC1-SFC7 Dimerization Module within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Hg1101
b:0.5
occ:0.39
|
SG
|
B:CYS84
|
2.5
|
63.1
|
0.3
|
HB1
|
A:ALA20
|
2.9
|
72.0
|
1.0
|
HB3
|
B:CYS84
|
3.1
|
81.3
|
0.7
|
HB2
|
B:CYS84
|
3.5
|
81.3
|
0.7
|
HB3
|
B:CYS84
|
3.7
|
80.0
|
0.3
|
CB
|
B:CYS84
|
3.7
|
67.7
|
0.7
|
CB
|
B:CYS84
|
3.7
|
66.6
|
0.3
|
H
|
A:ALA20
|
3.8
|
65.3
|
1.0
|
CB
|
A:ALA20
|
3.9
|
60.0
|
1.0
|
HB2
|
B:CYS84
|
3.9
|
80.0
|
0.3
|
HB2
|
A:ALA20
|
4.3
|
72.0
|
1.0
|
SG
|
B:CYS84
|
4.3
|
89.1
|
0.7
|
HB3
|
A:ALA20
|
4.4
|
72.0
|
1.0
|
N
|
A:ALA20
|
4.5
|
54.5
|
1.0
|
CA
|
A:ALA20
|
4.5
|
63.1
|
1.0
|
C
|
A:ALA20
|
4.5
|
69.9
|
1.0
|
O
|
A:ALA20
|
4.6
|
77.6
|
1.0
|
HB
|
B:THR10
|
4.6
|
0.5
|
1.0
|
HG13
|
B:VAL82
|
4.8
|
57.2
|
1.0
|
HG21
|
B:THR64
|
4.9
|
57.3
|
1.0
|
HG22
|
B:THR64
|
5.0
|
57.3
|
1.0
|
|
Reference:
N.M.I.Taylor,
F.Baudin,
G.Von Scheven,
C.W.Muller.
Rna Polymerase III-Specific General Transcription Factor Iiic Contains A Heterodimer Resembling Tfiif RAP30/RAP74. Nucleic Acids Res. V. 41 9183 2013.
ISSN: ISSN 0305-1048
PubMed: 23921640
DOI: 10.1093/NAR/GKT664
Page generated: Sun Aug 11 04:26:25 2024
|