Copper in PDB 6q6b: Structure of the Copper Storage Protein, Ccsp, From Streptomyces Lividans Loaded with 10 Copper Equivalents
Protein crystallography data
The structure of Structure of the Copper Storage Protein, Ccsp, From Streptomyces Lividans Loaded with 10 Copper Equivalents, PDB code: 6q6b
was solved by
M.L.Straw,
M.A.Hough,
J.A.R.Worrall,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
216.01 /
1.90
|
Space group
|
P 61 2 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
93.398,
93.398,
216.015,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
21.8 /
25.5
|
Copper Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
20;
Page 3, Binding sites: 21 -
30;
Page 4, Binding sites: 31 -
40;
Page 5, Binding sites: 41 -
50;
Page 6, Binding sites: 51 -
60;
Page 7, Binding sites: 61 -
64;
Binding sites:
The binding sites of Copper atom in the Structure of the Copper Storage Protein, Ccsp, From Streptomyces Lividans Loaded with 10 Copper Equivalents
(pdb code 6q6b). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 64 binding sites of Copper where determined in the
Structure of the Copper Storage Protein, Ccsp, From Streptomyces Lividans Loaded with 10 Copper Equivalents, PDB code: 6q6b:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Copper binding site 1 out
of 64 in 6q6b
Go back to
Copper Binding Sites List in 6q6b
Copper binding site 1 out
of 64 in the Structure of the Copper Storage Protein, Ccsp, From Streptomyces Lividans Loaded with 10 Copper Equivalents
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Structure of the Copper Storage Protein, Ccsp, From Streptomyces Lividans Loaded with 10 Copper Equivalents within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu201
b:75.9
occ:0.50
|
SG
|
B:CYS117
|
2.1
|
67.7
|
1.0
|
CU
|
B:CU1205
|
2.6
|
63.5
|
0.5
|
SG
|
B:CYS104
|
2.7
|
70.5
|
1.0
|
SG
|
B:CYS100
|
2.7
|
55.4
|
1.0
|
OD1
|
B:ASP61
|
3.1
|
47.8
|
1.0
|
CU
|
B:CU214
|
3.3
|
59.3
|
0.5
|
CB
|
B:CYS117
|
3.3
|
67.6
|
1.0
|
SG
|
B:CYS121
|
3.3
|
60.8
|
1.0
|
O
|
B:CYS100
|
3.7
|
45.0
|
1.0
|
CB
|
B:CYS104
|
3.8
|
63.7
|
1.0
|
CB
|
B:CYS100
|
3.8
|
51.8
|
1.0
|
C
|
B:CYS117
|
3.9
|
64.2
|
1.0
|
O
|
B:CYS117
|
3.9
|
53.2
|
1.0
|
SG
|
B:CYS38
|
4.0
|
57.3
|
1.0
|
C
|
B:CYS100
|
4.1
|
51.1
|
1.0
|
CA
|
B:CYS117
|
4.1
|
62.8
|
1.0
|
CU
|
B:CU1204
|
4.3
|
71.0
|
0.5
|
CG
|
B:ASP61
|
4.3
|
47.4
|
1.0
|
N
|
B:ALA118
|
4.3
|
63.6
|
1.0
|
CA
|
B:CYS100
|
4.5
|
53.0
|
1.0
|
N
|
B:GLY101
|
4.7
|
52.5
|
1.0
|
CB
|
B:CYS121
|
4.7
|
42.4
|
1.0
|
CA
|
B:ALA118
|
4.8
|
60.1
|
1.0
|
CU
|
B:CU1210
|
4.9
|
68.6
|
0.5
|
CB
|
B:CYS38
|
4.9
|
52.2
|
1.0
|
CA
|
B:CYS38
|
5.0
|
43.4
|
1.0
|
SG
|
B:CYS41
|
5.0
|
57.5
|
1.0
|
|
Copper binding site 2 out
of 64 in 6q6b
Go back to
Copper Binding Sites List in 6q6b
Copper binding site 2 out
of 64 in the Structure of the Copper Storage Protein, Ccsp, From Streptomyces Lividans Loaded with 10 Copper Equivalents
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Structure of the Copper Storage Protein, Ccsp, From Streptomyces Lividans Loaded with 10 Copper Equivalents within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu202
b:68.5
occ:1.00
|
ND1
|
B:HIS113
|
2.2
|
68.1
|
1.0
|
SG
|
B:CYS41
|
2.2
|
57.5
|
1.0
|
SG
|
B:CYS114
|
2.4
|
64.8
|
1.0
|
CE1
|
B:HIS113
|
3.1
|
60.4
|
1.0
|
N
|
B:CYS114
|
3.1
|
57.3
|
1.0
|
SG
|
B:CYS45
|
3.2
|
60.1
|
1.0
|
CG
|
B:HIS113
|
3.2
|
63.3
|
1.0
|
CU
|
B:CU1203
|
3.2
|
79.5
|
1.0
|
C
|
B:HIS113
|
3.4
|
63.5
|
1.0
|
CB
|
B:CYS41
|
3.5
|
46.8
|
1.0
|
CA
|
B:CYS114
|
3.5
|
55.7
|
1.0
|
CB
|
B:HIS113
|
3.5
|
60.8
|
1.0
|
CB
|
B:CYS114
|
3.5
|
57.8
|
1.0
|
O
|
B:CYS41
|
3.6
|
56.9
|
1.0
|
CA
|
B:CYS41
|
3.7
|
45.4
|
1.0
|
CU
|
B:CU214
|
3.8
|
59.3
|
0.5
|
O
|
B:HIS113
|
3.9
|
53.3
|
1.0
|
C
|
B:CYS41
|
4.0
|
45.7
|
1.0
|
CA
|
B:HIS113
|
4.0
|
63.9
|
1.0
|
NE2
|
B:HIS113
|
4.2
|
65.9
|
1.0
|
CD2
|
B:HIS113
|
4.3
|
63.6
|
1.0
|
CB
|
B:CYS45
|
4.6
|
47.1
|
1.0
|
N
|
B:CYS45
|
4.7
|
51.5
|
1.0
|
SG
|
B:CYS57
|
4.7
|
79.2
|
1.0
|
CB
|
B:ALA44
|
4.8
|
42.9
|
1.0
|
N
|
B:HIS113
|
4.9
|
62.0
|
1.0
|
CB
|
B:HIS111
|
5.0
|
70.3
|
1.0
|
C
|
B:CYS114
|
5.0
|
60.1
|
1.0
|
OD2
|
B:ASP61
|
5.0
|
47.2
|
1.0
|
|
Copper binding site 3 out
of 64 in 6q6b
Go back to
Copper Binding Sites List in 6q6b
Copper binding site 3 out
of 64 in the Structure of the Copper Storage Protein, Ccsp, From Streptomyces Lividans Loaded with 10 Copper Equivalents
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Structure of the Copper Storage Protein, Ccsp, From Streptomyces Lividans Loaded with 10 Copper Equivalents within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu203
b:79.5
occ:1.00
|
SG
|
B:CYS57
|
2.0
|
79.2
|
1.0
|
SG
|
B:CYS114
|
2.1
|
64.8
|
1.0
|
CU
|
B:CU1204
|
3.0
|
71.0
|
0.5
|
CU
|
B:CU1202
|
3.2
|
68.5
|
1.0
|
CB
|
B:CYS114
|
3.2
|
57.8
|
1.0
|
CU
|
B:CU214
|
3.3
|
59.3
|
0.5
|
SG
|
B:CYS45
|
3.3
|
60.1
|
1.0
|
CB
|
B:CYS57
|
3.4
|
66.4
|
1.0
|
SG
|
B:CYS41
|
3.5
|
57.5
|
1.0
|
SG
|
B:CYS104
|
3.9
|
70.5
|
1.0
|
ND1
|
B:HIS107
|
3.9
|
77.6
|
1.0
|
CB
|
B:HIS107
|
4.2
|
72.2
|
1.0
|
CA
|
B:CYS114
|
4.2
|
55.7
|
1.0
|
CA
|
B:CYS104
|
4.2
|
65.1
|
1.0
|
CG
|
B:HIS107
|
4.4
|
77.3
|
1.0
|
CB
|
B:CYS104
|
4.5
|
63.7
|
1.0
|
CA
|
B:CYS57
|
4.6
|
56.6
|
1.0
|
OD2
|
B:ASP61
|
4.8
|
47.2
|
1.0
|
N
|
B:CYS114
|
4.8
|
57.3
|
1.0
|
CD2
|
B:LEU54
|
4.9
|
60.7
|
1.0
|
O
|
B:CYS104
|
4.9
|
59.5
|
1.0
|
CE1
|
B:HIS107
|
4.9
|
79.6
|
1.0
|
ND1
|
B:HIS113
|
4.9
|
68.1
|
1.0
|
|
Copper binding site 4 out
of 64 in 6q6b
Go back to
Copper Binding Sites List in 6q6b
Copper binding site 4 out
of 64 in the Structure of the Copper Storage Protein, Ccsp, From Streptomyces Lividans Loaded with 10 Copper Equivalents
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of Structure of the Copper Storage Protein, Ccsp, From Streptomyces Lividans Loaded with 10 Copper Equivalents within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu204
b:71.0
occ:0.50
|
SG
|
B:CYS57
|
1.8
|
79.2
|
1.0
|
SG
|
B:CYS104
|
2.1
|
70.5
|
1.0
|
CU
|
B:CU214
|
2.6
|
59.3
|
0.5
|
CU
|
B:CU1203
|
3.0
|
79.5
|
1.0
|
CB
|
B:CYS57
|
3.1
|
66.4
|
1.0
|
OD1
|
B:ASP61
|
3.2
|
47.8
|
1.0
|
CA
|
B:CYS57
|
3.4
|
56.6
|
1.0
|
CB
|
B:CYS104
|
3.4
|
63.7
|
1.0
|
CA
|
B:CYS104
|
3.4
|
65.1
|
1.0
|
N
|
B:CYS104
|
3.5
|
56.8
|
1.0
|
O
|
B:CYS57
|
3.5
|
50.2
|
1.0
|
C
|
B:CYS57
|
3.8
|
51.4
|
1.0
|
CG
|
B:ASP61
|
3.8
|
47.4
|
1.0
|
OD2
|
B:ASP61
|
3.9
|
47.2
|
1.0
|
C
|
B:GLU103
|
4.1
|
61.5
|
1.0
|
CG
|
B:GLU103
|
4.2
|
63.8
|
1.0
|
SG
|
B:CYS41
|
4.2
|
57.5
|
1.0
|
CU
|
B:CU1201
|
4.3
|
75.9
|
0.5
|
O
|
B:CYS100
|
4.4
|
45.0
|
1.0
|
CB
|
B:GLU103
|
4.4
|
56.1
|
1.0
|
O
|
B:GLU103
|
4.5
|
53.8
|
1.0
|
SG
|
B:CYS100
|
4.6
|
55.4
|
1.0
|
SG
|
B:CYS114
|
4.7
|
64.8
|
1.0
|
N
|
B:CYS57
|
4.8
|
50.8
|
1.0
|
CA
|
B:GLU103
|
4.9
|
56.9
|
1.0
|
N
|
B:ILE58
|
4.9
|
42.6
|
1.0
|
C
|
B:CYS104
|
4.9
|
64.8
|
1.0
|
|
Copper binding site 5 out
of 64 in 6q6b
Go back to
Copper Binding Sites List in 6q6b
Copper binding site 5 out
of 64 in the Structure of the Copper Storage Protein, Ccsp, From Streptomyces Lividans Loaded with 10 Copper Equivalents
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 5 of Structure of the Copper Storage Protein, Ccsp, From Streptomyces Lividans Loaded with 10 Copper Equivalents within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu205
b:63.5
occ:0.50
|
SG
|
B:CYS38
|
2.1
|
57.3
|
1.0
|
SG
|
B:CYS100
|
2.2
|
55.4
|
1.0
|
CU
|
B:CU1201
|
2.6
|
75.9
|
0.5
|
SG
|
B:CYS121
|
2.8
|
60.8
|
1.0
|
CB
|
B:CYS100
|
3.0
|
51.8
|
1.0
|
CU
|
B:CU1210
|
3.1
|
68.6
|
0.5
|
CB
|
B:CYS64
|
3.3
|
43.1
|
1.0
|
CU
|
B:CU1207
|
3.4
|
46.5
|
0.5
|
CB
|
B:CYS38
|
3.4
|
52.2
|
1.0
|
SG
|
B:CYS117
|
3.5
|
67.7
|
1.0
|
SG
|
B:CYS64
|
3.6
|
56.0
|
1.0
|
OD1
|
B:ASP61
|
3.7
|
47.8
|
1.0
|
CA
|
B:ASP61
|
4.0
|
41.5
|
1.0
|
CA
|
B:CYS38
|
4.2
|
43.4
|
1.0
|
CA
|
B:CYS100
|
4.4
|
53.0
|
1.0
|
O
|
B:ASP61
|
4.5
|
38.8
|
1.0
|
O
|
B:THR60
|
4.5
|
40.5
|
1.0
|
CG
|
B:ASP61
|
4.6
|
47.4
|
1.0
|
CB
|
B:CYS121
|
4.6
|
42.4
|
1.0
|
C
|
B:CYS100
|
4.7
|
51.1
|
1.0
|
CB
|
B:ASP61
|
4.7
|
41.7
|
1.0
|
C
|
B:ASP61
|
4.8
|
33.9
|
1.0
|
N
|
B:ASP61
|
4.8
|
40.4
|
1.0
|
CA
|
B:CYS64
|
4.8
|
36.5
|
1.0
|
N
|
B:CYS38
|
4.9
|
46.7
|
1.0
|
O
|
B:CYS100
|
5.0
|
45.0
|
1.0
|
SG
|
B:CYS34
|
5.0
|
52.0
|
1.0
|
C
|
B:THR60
|
5.0
|
43.5
|
1.0
|
|
Copper binding site 6 out
of 64 in 6q6b
Go back to
Copper Binding Sites List in 6q6b
Copper binding site 6 out
of 64 in the Structure of the Copper Storage Protein, Ccsp, From Streptomyces Lividans Loaded with 10 Copper Equivalents
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 6 of Structure of the Copper Storage Protein, Ccsp, From Streptomyces Lividans Loaded with 10 Copper Equivalents within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu206
b:77.2
occ:1.00
|
SG
|
B:CYS124
|
2.2
|
58.3
|
1.0
|
SG
|
B:CYS128
|
2.2
|
55.8
|
1.0
|
CU
|
B:CU1211
|
2.3
|
51.8
|
0.5
|
O
|
B:CYS124
|
2.5
|
38.8
|
1.0
|
C
|
B:CYS124
|
3.1
|
43.5
|
1.0
|
CU
|
B:CU212
|
3.2
|
54.5
|
0.5
|
CB
|
B:CYS124
|
3.3
|
49.8
|
1.0
|
CB
|
B:CYS128
|
3.4
|
43.8
|
1.0
|
CA
|
B:CYS124
|
3.4
|
51.5
|
1.0
|
SG
|
B:CYS31
|
3.5
|
51.0
|
1.0
|
CU
|
B:CU1209
|
3.5
|
75.9
|
1.0
|
N
|
B:CYS128
|
3.9
|
39.1
|
1.0
|
N
|
B:GLU125
|
4.1
|
47.5
|
1.0
|
SG
|
B:CYS93
|
4.1
|
44.3
|
1.0
|
SG
|
B:CYS27
|
4.1
|
57.2
|
1.0
|
CA
|
B:CYS128
|
4.2
|
39.4
|
1.0
|
SG
|
B:CYS97
|
4.4
|
54.8
|
1.0
|
CA
|
B:GLU125
|
4.6
|
46.8
|
1.0
|
C
|
B:ALA127
|
4.9
|
42.9
|
1.0
|
CB
|
B:CYS31
|
4.9
|
46.7
|
1.0
|
N
|
B:CYS124
|
4.9
|
54.3
|
1.0
|
SG
|
B:CYS68
|
4.9
|
49.2
|
1.0
|
O
|
B:CYS27
|
4.9
|
37.1
|
1.0
|
N
|
B:CYS31
|
5.0
|
42.1
|
1.0
|
CB
|
B:ALA127
|
5.0
|
47.2
|
1.0
|
CA
|
B:CYS31
|
5.0
|
41.0
|
1.0
|
CU
|
B:CU213
|
5.0
|
70.8
|
0.5
|
CB
|
B:CYS93
|
5.0
|
36.5
|
1.0
|
|
Copper binding site 7 out
of 64 in 6q6b
Go back to
Copper Binding Sites List in 6q6b
Copper binding site 7 out
of 64 in the Structure of the Copper Storage Protein, Ccsp, From Streptomyces Lividans Loaded with 10 Copper Equivalents
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 7 of Structure of the Copper Storage Protein, Ccsp, From Streptomyces Lividans Loaded with 10 Copper Equivalents within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu207
b:46.5
occ:0.50
|
SG
|
B:CYS34
|
1.9
|
52.0
|
1.0
|
SG
|
B:CYS38
|
2.2
|
57.3
|
1.0
|
CU
|
B:CU1210
|
2.4
|
68.6
|
0.5
|
O
|
B:CYS34
|
2.6
|
42.5
|
1.0
|
C
|
B:CYS34
|
3.1
|
44.0
|
1.0
|
CB
|
B:CYS34
|
3.1
|
50.2
|
1.0
|
CU
|
B:CU213
|
3.2
|
70.8
|
0.5
|
SG
|
B:CYS121
|
3.3
|
60.8
|
1.0
|
CA
|
B:CYS34
|
3.3
|
41.5
|
1.0
|
CU
|
B:CU1205
|
3.4
|
63.5
|
0.5
|
CB
|
B:CYS38
|
3.6
|
52.2
|
1.0
|
CU
|
B:CU1208
|
3.7
|
80.4
|
1.0
|
SG
|
B:CYS64
|
3.8
|
56.0
|
1.0
|
N
|
B:ALA35
|
4.1
|
43.3
|
1.0
|
N
|
B:CYS38
|
4.2
|
46.7
|
1.0
|
CB
|
B:CYS64
|
4.4
|
43.1
|
1.0
|
CA
|
B:CYS38
|
4.4
|
43.4
|
1.0
|
CB
|
B:CYS121
|
4.5
|
42.4
|
1.0
|
CA
|
B:CYS121
|
4.5
|
45.4
|
1.0
|
N
|
B:CYS121
|
4.6
|
50.0
|
1.0
|
CA
|
B:ALA35
|
4.6
|
43.2
|
1.0
|
SG
|
B:CYS117
|
4.7
|
67.7
|
1.0
|
N
|
B:CYS34
|
4.8
|
43.0
|
1.0
|
SG
|
B:CYS68
|
4.8
|
49.2
|
1.0
|
CB
|
B:ALA120
|
4.9
|
53.7
|
1.0
|
CB
|
B:ALA37
|
5.0
|
46.2
|
1.0
|
SG
|
B:CYS97
|
5.0
|
54.8
|
1.0
|
C
|
B:ALA120
|
5.0
|
51.0
|
1.0
|
|
Copper binding site 8 out
of 64 in 6q6b
Go back to
Copper Binding Sites List in 6q6b
Copper binding site 8 out
of 64 in the Structure of the Copper Storage Protein, Ccsp, From Streptomyces Lividans Loaded with 10 Copper Equivalents
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 8 of Structure of the Copper Storage Protein, Ccsp, From Streptomyces Lividans Loaded with 10 Copper Equivalents within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu208
b:80.4
occ:1.00
|
SG
|
B:CYS68
|
2.1
|
49.2
|
1.0
|
SG
|
B:CYS64
|
2.4
|
56.0
|
1.0
|
O
|
B:CYS64
|
2.4
|
39.1
|
1.0
|
CU
|
B:CU213
|
2.8
|
70.8
|
0.5
|
C
|
B:CYS64
|
3.0
|
36.5
|
1.0
|
CB
|
B:CYS68
|
3.1
|
38.0
|
1.0
|
CU
|
B:CU1210
|
3.2
|
68.6
|
0.5
|
CB
|
B:CYS64
|
3.3
|
43.1
|
1.0
|
CA
|
B:CYS64
|
3.4
|
36.5
|
1.0
|
SG
|
B:CYS97
|
3.4
|
54.8
|
1.0
|
CU
|
B:CU212
|
3.4
|
54.5
|
0.5
|
CU
|
B:CU1207
|
3.7
|
46.5
|
0.5
|
SG
|
B:CYS34
|
3.8
|
52.0
|
1.0
|
CU
|
B:CU1209
|
3.9
|
75.9
|
1.0
|
N
|
B:CYS68
|
3.9
|
32.8
|
1.0
|
N
|
B:ALA65
|
4.0
|
38.9
|
1.0
|
CA
|
B:CYS68
|
4.0
|
31.7
|
1.0
|
CB
|
B:CYS34
|
4.4
|
50.2
|
1.0
|
CG1
|
B:VAL96
|
4.5
|
46.5
|
0.5
|
SG
|
B:CYS38
|
4.6
|
57.3
|
1.0
|
CA
|
B:ALA65
|
4.6
|
38.0
|
1.0
|
N
|
B:CYS64
|
4.8
|
40.7
|
1.0
|
SG
|
B:CYS93
|
4.8
|
44.3
|
1.0
|
CB
|
B:CYS97
|
4.9
|
48.1
|
1.0
|
C
|
B:CYS34
|
4.9
|
44.0
|
1.0
|
N
|
B:ALA35
|
5.0
|
43.3
|
1.0
|
|
Copper binding site 9 out
of 64 in 6q6b
Go back to
Copper Binding Sites List in 6q6b
Copper binding site 9 out
of 64 in the Structure of the Copper Storage Protein, Ccsp, From Streptomyces Lividans Loaded with 10 Copper Equivalents
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 9 of Structure of the Copper Storage Protein, Ccsp, From Streptomyces Lividans Loaded with 10 Copper Equivalents within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu209
b:75.9
occ:1.00
|
SG
|
B:CYS97
|
2.2
|
54.8
|
1.0
|
SG
|
B:CYS93
|
2.3
|
44.3
|
1.0
|
O
|
B:CYS93
|
2.6
|
37.2
|
1.0
|
CU
|
B:CU1211
|
2.8
|
51.8
|
0.5
|
CU
|
B:CU212
|
2.8
|
54.5
|
0.5
|
C
|
B:CYS93
|
3.1
|
42.1
|
1.0
|
SG
|
B:CYS68
|
3.2
|
49.2
|
1.0
|
CB
|
B:CYS97
|
3.3
|
48.1
|
1.0
|
CB
|
B:CYS93
|
3.3
|
36.5
|
1.0
|
CA
|
B:CYS93
|
3.5
|
38.6
|
1.0
|
CU
|
B:CU1206
|
3.5
|
77.2
|
1.0
|
CU
|
B:CU213
|
3.6
|
70.8
|
0.5
|
CU
|
B:CU1208
|
3.9
|
80.4
|
1.0
|
SG
|
B:CYS124
|
3.9
|
58.3
|
1.0
|
N
|
B:ALA94
|
4.0
|
43.7
|
1.0
|
N
|
B:CYS97
|
4.1
|
43.2
|
1.0
|
CG1
|
B:VAL96
|
4.1
|
46.5
|
0.5
|
CA
|
B:CYS97
|
4.2
|
49.0
|
1.0
|
SG
|
B:CYS128
|
4.5
|
55.8
|
1.0
|
CA
|
B:ALA94
|
4.6
|
43.5
|
1.0
|
CB
|
B:CYS124
|
4.7
|
49.8
|
1.0
|
SG
|
B:CYS64
|
4.8
|
56.0
|
1.0
|
CB
|
B:CYS68
|
4.8
|
38.0
|
1.0
|
N
|
B:CYS93
|
4.9
|
35.4
|
1.0
|
|
Copper binding site 10 out
of 64 in 6q6b
Go back to
Copper Binding Sites List in 6q6b
Copper binding site 10 out
of 64 in the Structure of the Copper Storage Protein, Ccsp, From Streptomyces Lividans Loaded with 10 Copper Equivalents
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 10 of Structure of the Copper Storage Protein, Ccsp, From Streptomyces Lividans Loaded with 10 Copper Equivalents within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu210
b:68.6
occ:0.50
|
SG
|
B:CYS64
|
2.2
|
56.0
|
1.0
|
SG
|
B:CYS121
|
2.3
|
60.8
|
1.0
|
CU
|
B:CU1207
|
2.4
|
46.5
|
0.5
|
CU
|
B:CU213
|
2.4
|
70.8
|
0.5
|
SG
|
B:CYS34
|
2.8
|
52.0
|
1.0
|
CU
|
B:CU1205
|
3.1
|
63.5
|
0.5
|
CU
|
B:CU1208
|
3.2
|
80.4
|
1.0
|
CB
|
B:CYS121
|
3.3
|
42.4
|
1.0
|
SG
|
B:CYS38
|
3.3
|
57.3
|
1.0
|
SG
|
B:CYS97
|
3.4
|
54.8
|
1.0
|
CB
|
B:CYS64
|
3.4
|
43.1
|
1.0
|
CA
|
B:CYS121
|
3.7
|
45.4
|
1.0
|
CA
|
B:CYS97
|
3.8
|
49.0
|
1.0
|
CB
|
B:CYS100
|
4.0
|
51.8
|
1.0
|
CB
|
B:CYS97
|
4.0
|
48.1
|
1.0
|
CB
|
B:CYS34
|
4.4
|
50.2
|
1.0
|
SG
|
B:CYS100
|
4.5
|
55.4
|
1.0
|
N
|
B:CYS121
|
4.5
|
50.0
|
1.0
|
O
|
B:CYS97
|
4.5
|
53.8
|
1.0
|
CA
|
B:CYS64
|
4.7
|
36.5
|
1.0
|
SG
|
B:CYS68
|
4.7
|
49.2
|
1.0
|
C
|
B:CYS97
|
4.7
|
50.5
|
1.0
|
N
|
B:CYS97
|
4.7
|
43.2
|
1.0
|
C
|
B:CYS121
|
4.9
|
48.9
|
1.0
|
CU
|
B:CU1201
|
4.9
|
75.9
|
0.5
|
O
|
B:CYS34
|
4.9
|
42.5
|
1.0
|
O
|
B:VAL96
|
5.0
|
48.6
|
0.5
|
O
|
B:VAL96
|
5.0
|
51.2
|
0.5
|
C
|
B:CYS64
|
5.0
|
36.5
|
1.0
|
O
|
B:CYS121
|
5.0
|
49.1
|
1.0
|
|
Reference:
M.L.Straw,
M.A.Hough,
M.T.Wilson,
J.A.R.Worrall.
A Histidine Residue and A Tetranuclear Cuprous-Thiolate Cluster Dominate the Copper Loading Landscape of A Copper Storage Protein From Streptomyces Lividans. Chemistry V. 25 10678 2019.
ISSN: ISSN 0947-6539
PubMed: 31111982
DOI: 10.1002/CHEM.201901411
Page generated: Wed Jul 31 06:47:00 2024
|