Copper in PDB 8p3l: The Structure of Thiocyanate Dehydrogenase Mutant Form with Thr 169 Replaced By Ala From Thioalkalivibrio Paradoxus
Protein crystallography data
The structure of The Structure of Thiocyanate Dehydrogenase Mutant Form with Thr 169 Replaced By Ala From Thioalkalivibrio Paradoxus, PDB code: 8p3l
was solved by
L.A.Varfolomeeva,
K.M.Polyakov,
A.S.Komolov,
T.V.Rakitina,
N.I.Dergousova,
P.V.Dorovatovskii,
K.M.Boyko,
T.V.Tikhonova,
V.O.Popov,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
81.12 /
1.80
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
90.81,
162.24,
90.76,
90,
119.74,
90
|
R / Rfree (%)
|
18.6 /
25.4
|
Copper Binding Sites:
The binding sites of Copper atom in the The Structure of Thiocyanate Dehydrogenase Mutant Form with Thr 169 Replaced By Ala From Thioalkalivibrio Paradoxus
(pdb code 8p3l). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 10 binding sites of Copper where determined in the
The Structure of Thiocyanate Dehydrogenase Mutant Form with Thr 169 Replaced By Ala From Thioalkalivibrio Paradoxus, PDB code: 8p3l:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Copper binding site 1 out
of 10 in 8p3l
Go back to
Copper Binding Sites List in 8p3l
Copper binding site 1 out
of 10 in the The Structure of Thiocyanate Dehydrogenase Mutant Form with Thr 169 Replaced By Ala From Thioalkalivibrio Paradoxus
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of The Structure of Thiocyanate Dehydrogenase Mutant Form with Thr 169 Replaced By Ala From Thioalkalivibrio Paradoxus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu601
b:15.7
occ:1.00
|
O
|
A:HOH702
|
1.9
|
9.4
|
1.0
|
NE2
|
A:HIS206
|
2.0
|
13.3
|
1.0
|
NE2
|
A:HIS381
|
2.1
|
27.8
|
1.0
|
OD1
|
A:ASP314
|
2.4
|
18.0
|
1.0
|
OD2
|
A:ASP314
|
2.9
|
17.8
|
1.0
|
CG
|
A:ASP314
|
2.9
|
19.4
|
1.0
|
CE1
|
A:HIS206
|
3.0
|
14.4
|
1.0
|
CE1
|
A:HIS381
|
3.1
|
27.2
|
1.0
|
CD2
|
A:HIS206
|
3.1
|
12.5
|
1.0
|
CD2
|
A:HIS381
|
3.1
|
29.7
|
1.0
|
O4
|
A:SO4603
|
4.1
|
8.5
|
0.5
|
ND1
|
A:HIS206
|
4.1
|
11.3
|
1.0
|
ND1
|
A:HIS381
|
4.2
|
25.8
|
1.0
|
O
|
A:HOH770
|
4.2
|
5.7
|
1.0
|
CG
|
A:HIS206
|
4.2
|
11.9
|
1.0
|
CG
|
A:HIS381
|
4.2
|
29.5
|
1.0
|
OG1
|
A:THR548
|
4.4
|
25.2
|
1.0
|
CB
|
A:ASP314
|
4.4
|
15.1
|
1.0
|
O
|
A:HOH717
|
4.8
|
14.8
|
1.0
|
CE1
|
A:HIS437
|
4.9
|
11.4
|
1.0
|
CG1
|
A:VAL205
|
4.9
|
10.1
|
1.0
|
O
|
A:PHE436
|
5.0
|
12.3
|
1.0
|
|
Copper binding site 2 out
of 10 in 8p3l
Go back to
Copper Binding Sites List in 8p3l
Copper binding site 2 out
of 10 in the The Structure of Thiocyanate Dehydrogenase Mutant Form with Thr 169 Replaced By Ala From Thioalkalivibrio Paradoxus
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of The Structure of Thiocyanate Dehydrogenase Mutant Form with Thr 169 Replaced By Ala From Thioalkalivibrio Paradoxus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu602
b:22.4
occ:1.00
|
ND1
|
A:HIS528
|
1.8
|
11.8
|
1.0
|
NZ
|
A:LYS103
|
1.9
|
22.6
|
1.0
|
NE2
|
A:HIS135
|
1.9
|
10.2
|
1.0
|
O
|
A:HOH757
|
2.5
|
3.5
|
0.5
|
CE1
|
A:HIS528
|
2.8
|
13.4
|
1.0
|
CG
|
A:HIS528
|
2.8
|
13.6
|
1.0
|
CD2
|
A:HIS135
|
2.9
|
12.1
|
1.0
|
CE1
|
A:HIS135
|
3.0
|
9.6
|
1.0
|
CB
|
A:HIS528
|
3.2
|
11.8
|
1.0
|
CE
|
A:LYS103
|
3.3
|
22.3
|
1.0
|
O
|
A:HOH782
|
3.4
|
4.7
|
0.5
|
O
|
A:HOH770
|
3.6
|
5.7
|
1.0
|
NE2
|
A:HIS528
|
3.9
|
12.4
|
1.0
|
CD2
|
A:HIS528
|
3.9
|
15.5
|
1.0
|
CD
|
A:LYS103
|
4.0
|
22.1
|
1.0
|
O2
|
A:SO4603
|
4.0
|
8.4
|
0.5
|
ND1
|
A:HIS135
|
4.0
|
13.8
|
1.0
|
CG
|
A:HIS135
|
4.0
|
15.2
|
1.0
|
OH
|
A:TYR164
|
4.1
|
30.3
|
1.0
|
NE2
|
A:HIS136
|
4.1
|
12.1
|
1.0
|
OE1
|
A:GLU288
|
4.2
|
19.9
|
1.0
|
CE1
|
A:HIS136
|
4.5
|
10.5
|
1.0
|
CA
|
A:HIS528
|
4.8
|
14.2
|
1.0
|
OE1
|
A:GLN156
|
4.8
|
19.2
|
1.0
|
O
|
A:HOH800
|
4.9
|
17.7
|
1.0
|
O
|
A:HOH775
|
5.0
|
10.3
|
1.0
|
|
Copper binding site 3 out
of 10 in 8p3l
Go back to
Copper Binding Sites List in 8p3l
Copper binding site 3 out
of 10 in the The Structure of Thiocyanate Dehydrogenase Mutant Form with Thr 169 Replaced By Ala From Thioalkalivibrio Paradoxus
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of The Structure of Thiocyanate Dehydrogenase Mutant Form with Thr 169 Replaced By Ala From Thioalkalivibrio Paradoxus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cu601
b:18.9
occ:1.00
|
NE2
|
D:HIS206
|
2.1
|
19.8
|
1.0
|
NE2
|
D:HIS381
|
2.1
|
10.0
|
1.0
|
OD1
|
D:ASP314
|
2.3
|
12.5
|
1.0
|
OD2
|
D:ASP314
|
2.3
|
9.1
|
1.0
|
CG
|
D:ASP314
|
2.6
|
13.1
|
1.0
|
O
|
D:HOH732
|
2.7
|
17.9
|
1.0
|
CD2
|
D:HIS381
|
2.9
|
11.7
|
1.0
|
CE1
|
D:HIS206
|
3.0
|
17.1
|
1.0
|
CD2
|
D:HIS206
|
3.2
|
15.5
|
1.0
|
CE1
|
D:HIS381
|
3.2
|
10.3
|
1.0
|
CB
|
D:ASP314
|
4.1
|
13.6
|
1.0
|
CG
|
D:HIS381
|
4.1
|
14.4
|
1.0
|
ND1
|
D:HIS206
|
4.1
|
21.8
|
1.0
|
ND1
|
D:HIS381
|
4.2
|
12.5
|
1.0
|
O3
|
D:SO4604
|
4.2
|
12.2
|
0.7
|
CG
|
D:HIS206
|
4.3
|
17.6
|
1.0
|
OG1
|
D:THR548
|
4.5
|
15.9
|
1.0
|
O
|
D:HOH753
|
4.5
|
11.4
|
1.0
|
O
|
D:HOH767
|
4.6
|
1.5
|
0.2
|
CE1
|
D:HIS437
|
4.8
|
21.7
|
1.0
|
O
|
D:PHE436
|
4.9
|
14.7
|
1.0
|
O
|
D:HOH711
|
4.9
|
11.9
|
1.0
|
O
|
D:ASP314
|
4.9
|
17.7
|
1.0
|
|
Copper binding site 4 out
of 10 in 8p3l
Go back to
Copper Binding Sites List in 8p3l
Copper binding site 4 out
of 10 in the The Structure of Thiocyanate Dehydrogenase Mutant Form with Thr 169 Replaced By Ala From Thioalkalivibrio Paradoxus
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of The Structure of Thiocyanate Dehydrogenase Mutant Form with Thr 169 Replaced By Ala From Thioalkalivibrio Paradoxus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cu602
b:14.7
occ:0.80
|
CU
|
D:CU602
|
0.0
|
14.7
|
0.8
|
CU
|
D:CU602
|
1.1
|
6.2
|
0.2
|
ND1
|
D:HIS528
|
1.7
|
5.1
|
1.0
|
O
|
D:HOH747
|
1.9
|
5.6
|
0.8
|
NE2
|
D:HIS135
|
2.0
|
11.2
|
1.0
|
CE1
|
D:HIS528
|
2.4
|
5.0
|
1.0
|
NZ
|
D:LYS103
|
2.8
|
15.0
|
1.0
|
CD2
|
D:HIS135
|
2.8
|
21.4
|
1.0
|
CG
|
D:HIS528
|
2.9
|
7.1
|
1.0
|
CE1
|
D:HIS135
|
3.0
|
14.2
|
1.0
|
CE
|
D:LYS103
|
3.1
|
10.1
|
1.0
|
O
|
D:HOH767
|
3.4
|
1.5
|
0.2
|
CB
|
D:HIS528
|
3.6
|
9.4
|
1.0
|
NE2
|
D:HIS528
|
3.7
|
8.3
|
1.0
|
CD
|
D:LYS103
|
3.8
|
15.8
|
1.0
|
OH
|
D:TYR164
|
3.9
|
20.8
|
1.0
|
CD2
|
D:HIS528
|
3.9
|
6.3
|
1.0
|
CG
|
D:HIS135
|
4.0
|
18.3
|
1.0
|
OE1
|
D:GLN156
|
4.0
|
17.3
|
1.0
|
ND1
|
D:HIS135
|
4.0
|
18.7
|
1.0
|
OE1
|
D:GLU288
|
4.2
|
9.6
|
1.0
|
O4
|
D:SO4604
|
4.3
|
13.3
|
0.7
|
O
|
D:HOH712
|
4.3
|
9.9
|
1.0
|
NE2
|
D:HIS136
|
4.3
|
10.4
|
1.0
|
CE1
|
D:HIS136
|
4.5
|
16.2
|
1.0
|
CD
|
D:GLN156
|
4.9
|
16.0
|
1.0
|
OE2
|
D:GLU288
|
5.0
|
13.1
|
1.0
|
|
Copper binding site 5 out
of 10 in 8p3l
Go back to
Copper Binding Sites List in 8p3l
Copper binding site 5 out
of 10 in the The Structure of Thiocyanate Dehydrogenase Mutant Form with Thr 169 Replaced By Ala From Thioalkalivibrio Paradoxus
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 5 of The Structure of Thiocyanate Dehydrogenase Mutant Form with Thr 169 Replaced By Ala From Thioalkalivibrio Paradoxus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cu602
b:6.2
occ:0.20
|
CU
|
D:CU602
|
0.0
|
6.2
|
0.2
|
O
|
D:HOH747
|
0.9
|
5.6
|
0.8
|
CU
|
D:CU602
|
1.1
|
14.7
|
0.8
|
ND1
|
D:HIS528
|
1.8
|
5.1
|
1.0
|
NE2
|
D:HIS135
|
2.1
|
11.2
|
1.0
|
CE1
|
D:HIS528
|
2.6
|
5.0
|
1.0
|
O
|
D:HOH767
|
2.7
|
1.5
|
0.2
|
CG
|
D:HIS528
|
2.8
|
7.1
|
1.0
|
CE1
|
D:HIS135
|
3.1
|
14.2
|
1.0
|
CD2
|
D:HIS135
|
3.2
|
21.4
|
1.0
|
CB
|
D:HIS528
|
3.3
|
9.4
|
1.0
|
O4
|
D:SO4604
|
3.5
|
13.3
|
0.7
|
NE2
|
D:HIS136
|
3.7
|
10.4
|
1.0
|
CE1
|
D:HIS136
|
3.8
|
16.2
|
1.0
|
NE2
|
D:HIS528
|
3.8
|
8.3
|
1.0
|
CD2
|
D:HIS528
|
3.8
|
6.3
|
1.0
|
NZ
|
D:LYS103
|
3.9
|
15.0
|
1.0
|
CE
|
D:LYS103
|
4.1
|
10.1
|
1.0
|
ND1
|
D:HIS135
|
4.3
|
18.7
|
1.0
|
O
|
D:HOH814
|
4.3
|
13.4
|
1.0
|
CG
|
D:HIS135
|
4.3
|
18.3
|
1.0
|
OE1
|
D:GLU288
|
4.4
|
9.6
|
1.0
|
CA
|
D:HIS528
|
4.6
|
11.6
|
1.0
|
O
|
D:HOH732
|
4.7
|
17.9
|
1.0
|
OE2
|
D:GLU288
|
4.7
|
13.1
|
1.0
|
CD
|
D:LYS103
|
4.7
|
15.8
|
1.0
|
OH
|
D:TYR164
|
4.7
|
20.8
|
1.0
|
S
|
D:SO4604
|
4.8
|
14.1
|
0.7
|
OE1
|
D:GLN156
|
4.8
|
17.3
|
1.0
|
O
|
D:HIS528
|
4.8
|
15.3
|
1.0
|
O3
|
D:SO4604
|
4.9
|
12.2
|
0.7
|
CD2
|
D:HIS136
|
4.9
|
14.5
|
1.0
|
ND1
|
D:HIS136
|
4.9
|
18.4
|
1.0
|
CD
|
D:GLU288
|
5.0
|
12.3
|
1.0
|
|
Copper binding site 6 out
of 10 in 8p3l
Go back to
Copper Binding Sites List in 8p3l
Copper binding site 6 out
of 10 in the The Structure of Thiocyanate Dehydrogenase Mutant Form with Thr 169 Replaced By Ala From Thioalkalivibrio Paradoxus
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 6 of The Structure of Thiocyanate Dehydrogenase Mutant Form with Thr 169 Replaced By Ala From Thioalkalivibrio Paradoxus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Cu601
b:12.7
occ:1.00
|
O
|
G:HOH748
|
1.9
|
8.8
|
1.0
|
O
|
G:HOH741
|
1.9
|
4.8
|
0.5
|
NE2
|
G:HIS206
|
1.9
|
7.5
|
1.0
|
NE2
|
G:HIS381
|
2.0
|
9.4
|
1.0
|
OD1
|
G:ASP314
|
2.2
|
9.5
|
1.0
|
OD2
|
G:ASP314
|
2.8
|
18.8
|
1.0
|
CG
|
G:ASP314
|
2.8
|
20.6
|
1.0
|
CE1
|
G:HIS206
|
2.8
|
8.1
|
1.0
|
CD2
|
G:HIS206
|
3.0
|
7.8
|
1.0
|
CE1
|
G:HIS381
|
3.0
|
11.0
|
1.0
|
CD2
|
G:HIS381
|
3.0
|
13.8
|
1.0
|
O
|
G:HOH733
|
3.9
|
7.7
|
0.5
|
ND1
|
G:HIS206
|
3.9
|
8.2
|
1.0
|
CG
|
G:HIS206
|
4.0
|
10.1
|
1.0
|
OG1
|
G:THR548
|
4.1
|
18.4
|
1.0
|
ND1
|
G:HIS381
|
4.1
|
12.4
|
1.0
|
CG
|
G:HIS381
|
4.1
|
12.9
|
1.0
|
O4
|
G:SO4606
|
4.2
|
18.8
|
1.0
|
CB
|
G:ASP314
|
4.3
|
17.6
|
1.0
|
O
|
G:HOH723
|
4.6
|
10.3
|
1.0
|
CE1
|
G:HIS437
|
4.6
|
14.7
|
1.0
|
O
|
G:PHE436
|
4.7
|
21.9
|
1.0
|
NE2
|
G:HIS136
|
4.9
|
13.1
|
1.0
|
CE1
|
G:HIS136
|
4.9
|
13.5
|
1.0
|
CG1
|
G:VAL205
|
5.0
|
17.5
|
1.0
|
|
Copper binding site 7 out
of 10 in 8p3l
Go back to
Copper Binding Sites List in 8p3l
Copper binding site 7 out
of 10 in the The Structure of Thiocyanate Dehydrogenase Mutant Form with Thr 169 Replaced By Ala From Thioalkalivibrio Paradoxus
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 7 of The Structure of Thiocyanate Dehydrogenase Mutant Form with Thr 169 Replaced By Ala From Thioalkalivibrio Paradoxus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Cu602
b:17.1
occ:0.70
|
CU
|
G:CU602
|
0.0
|
17.1
|
0.7
|
CU
|
G:CU602
|
0.7
|
15.1
|
0.3
|
NZ
|
G:LYS103
|
1.6
|
17.8
|
1.0
|
ND1
|
G:HIS528
|
1.7
|
23.7
|
1.0
|
O
|
G:HOH766
|
1.9
|
13.5
|
0.8
|
NE2
|
G:HIS135
|
1.9
|
14.5
|
1.0
|
CE1
|
G:HIS528
|
2.7
|
24.5
|
1.0
|
CG
|
G:HIS528
|
2.8
|
27.4
|
1.0
|
CD2
|
G:HIS135
|
2.9
|
10.5
|
1.0
|
CE1
|
G:HIS135
|
3.0
|
10.2
|
1.0
|
CE
|
G:LYS103
|
3.1
|
11.9
|
1.0
|
CB
|
G:HIS528
|
3.2
|
22.7
|
1.0
|
CD
|
G:LYS103
|
3.6
|
12.9
|
1.0
|
NE2
|
G:HIS528
|
3.9
|
23.9
|
1.0
|
CD2
|
G:HIS528
|
3.9
|
26.7
|
1.0
|
CG
|
G:HIS135
|
4.0
|
9.0
|
1.0
|
ND1
|
G:HIS135
|
4.0
|
9.8
|
1.0
|
O
|
G:HOH733
|
4.0
|
7.7
|
0.5
|
O1
|
G:SO4606
|
4.1
|
22.2
|
1.0
|
OH
|
G:TYR164
|
4.2
|
43.3
|
1.0
|
OE1
|
G:GLN156
|
4.3
|
19.6
|
1.0
|
OE1
|
G:GLU288
|
4.3
|
11.4
|
1.0
|
NE2
|
G:HIS136
|
4.4
|
13.1
|
1.0
|
CA
|
G:HIS528
|
4.7
|
22.7
|
1.0
|
O
|
G:HOH732
|
4.9
|
18.1
|
1.0
|
CE1
|
G:HIS136
|
4.9
|
13.5
|
1.0
|
|
Copper binding site 8 out
of 10 in 8p3l
Go back to
Copper Binding Sites List in 8p3l
Copper binding site 8 out
of 10 in the The Structure of Thiocyanate Dehydrogenase Mutant Form with Thr 169 Replaced By Ala From Thioalkalivibrio Paradoxus
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 8 of The Structure of Thiocyanate Dehydrogenase Mutant Form with Thr 169 Replaced By Ala From Thioalkalivibrio Paradoxus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Cu602
b:15.1
occ:0.30
|
CU
|
G:CU602
|
0.0
|
15.1
|
0.3
|
CU
|
G:CU602
|
0.7
|
17.1
|
0.7
|
ND1
|
G:HIS528
|
1.8
|
23.7
|
1.0
|
O
|
G:HOH766
|
1.9
|
13.5
|
0.8
|
NE2
|
G:HIS135
|
2.1
|
14.5
|
1.0
|
NZ
|
G:LYS103
|
2.3
|
17.8
|
1.0
|
CG
|
G:HIS528
|
2.8
|
27.4
|
1.0
|
CE1
|
G:HIS528
|
2.8
|
24.5
|
1.0
|
CE1
|
G:HIS135
|
3.1
|
10.2
|
1.0
|
CB
|
G:HIS528
|
3.2
|
22.7
|
1.0
|
CD2
|
G:HIS135
|
3.2
|
10.5
|
1.0
|
O
|
G:HOH733
|
3.4
|
7.7
|
0.5
|
O1
|
G:SO4606
|
3.6
|
22.2
|
1.0
|
CE
|
G:LYS103
|
3.8
|
11.9
|
1.0
|
CD2
|
G:HIS528
|
3.9
|
26.7
|
1.0
|
NE2
|
G:HIS528
|
4.0
|
23.9
|
1.0
|
NE2
|
G:HIS136
|
4.0
|
13.1
|
1.0
|
ND1
|
G:HIS135
|
4.2
|
9.8
|
1.0
|
CD
|
G:LYS103
|
4.2
|
12.9
|
1.0
|
O
|
G:HOH732
|
4.2
|
18.1
|
1.0
|
CG
|
G:HIS135
|
4.3
|
9.0
|
1.0
|
OE1
|
G:GLU288
|
4.3
|
11.4
|
1.0
|
CE1
|
G:HIS136
|
4.4
|
13.5
|
1.0
|
CA
|
G:HIS528
|
4.6
|
22.7
|
1.0
|
OH
|
G:TYR164
|
4.6
|
43.3
|
1.0
|
CD2
|
G:HIS136
|
4.8
|
12.2
|
1.0
|
OE1
|
G:GLN156
|
4.8
|
19.6
|
1.0
|
S
|
G:SO4606
|
4.8
|
19.6
|
1.0
|
|
Copper binding site 9 out
of 10 in 8p3l
Go back to
Copper Binding Sites List in 8p3l
Copper binding site 9 out
of 10 in the The Structure of Thiocyanate Dehydrogenase Mutant Form with Thr 169 Replaced By Ala From Thioalkalivibrio Paradoxus
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 9 of The Structure of Thiocyanate Dehydrogenase Mutant Form with Thr 169 Replaced By Ala From Thioalkalivibrio Paradoxus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
J:Cu601
b:23.3
occ:1.00
|
O
|
J:HOH711
|
1.9
|
21.9
|
1.0
|
NE2
|
J:HIS381
|
2.0
|
11.8
|
1.0
|
NE2
|
J:HIS206
|
2.1
|
13.3
|
1.0
|
OD2
|
J:ASP314
|
2.3
|
21.7
|
1.0
|
OD1
|
J:ASP314
|
2.8
|
23.4
|
1.0
|
CD2
|
J:HIS206
|
2.8
|
14.5
|
1.0
|
CD2
|
J:HIS381
|
2.9
|
13.6
|
1.0
|
CG
|
J:ASP314
|
2.9
|
20.5
|
1.0
|
CE1
|
J:HIS381
|
3.0
|
13.9
|
1.0
|
CE1
|
J:HIS206
|
3.2
|
13.3
|
1.0
|
ND1
|
J:HIS381
|
4.0
|
16.1
|
1.0
|
CG
|
J:HIS381
|
4.0
|
12.8
|
1.0
|
CG
|
J:HIS206
|
4.0
|
18.5
|
1.0
|
O
|
J:HOH708
|
4.1
|
28.9
|
1.0
|
ND1
|
J:HIS206
|
4.2
|
21.9
|
1.0
|
O
|
J:HOH714
|
4.2
|
13.5
|
1.0
|
O1
|
J:SO4603
|
4.4
|
23.9
|
1.0
|
CB
|
J:ASP314
|
4.4
|
23.1
|
1.0
|
O
|
J:HOH773
|
4.4
|
17.1
|
1.0
|
OG1
|
J:THR548
|
4.6
|
14.9
|
1.0
|
O
|
J:PHE436
|
4.7
|
21.8
|
1.0
|
CE1
|
J:HIS437
|
4.9
|
18.8
|
1.0
|
NE2
|
J:HIS136
|
5.0
|
24.9
|
1.0
|
|
Copper binding site 10 out
of 10 in 8p3l
Go back to
Copper Binding Sites List in 8p3l
Copper binding site 10 out
of 10 in the The Structure of Thiocyanate Dehydrogenase Mutant Form with Thr 169 Replaced By Ala From Thioalkalivibrio Paradoxus
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 10 of The Structure of Thiocyanate Dehydrogenase Mutant Form with Thr 169 Replaced By Ala From Thioalkalivibrio Paradoxus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
J:Cu602
b:19.9
occ:1.00
|
O
|
J:HOH734
|
1.8
|
11.2
|
1.0
|
ND1
|
J:HIS528
|
1.9
|
7.3
|
1.0
|
NZ
|
J:LYS103
|
1.9
|
16.1
|
1.0
|
NE2
|
J:HIS135
|
2.2
|
20.1
|
1.0
|
CE1
|
J:HIS528
|
2.9
|
6.0
|
1.0
|
CD2
|
J:HIS135
|
2.9
|
19.3
|
1.0
|
CG
|
J:HIS528
|
3.0
|
7.1
|
1.0
|
CE
|
J:LYS103
|
3.2
|
24.1
|
1.0
|
CB
|
J:HIS528
|
3.3
|
11.3
|
1.0
|
CE1
|
J:HIS135
|
3.4
|
17.1
|
1.0
|
O
|
J:HOH708
|
3.7
|
28.9
|
1.0
|
CD
|
J:LYS103
|
3.8
|
20.6
|
1.0
|
NE2
|
J:HIS528
|
4.0
|
5.6
|
1.0
|
CD2
|
J:HIS528
|
4.0
|
6.5
|
1.0
|
O2
|
J:SO4603
|
4.1
|
18.2
|
1.0
|
OE1
|
J:GLU288
|
4.1
|
21.3
|
1.0
|
CG
|
J:HIS135
|
4.1
|
17.4
|
1.0
|
OH
|
J:TYR164
|
4.3
|
42.1
|
1.0
|
NE2
|
J:HIS136
|
4.3
|
24.9
|
1.0
|
ND1
|
J:HIS135
|
4.4
|
16.5
|
1.0
|
OE1
|
J:GLN156
|
4.5
|
12.8
|
1.0
|
O
|
J:HOH784
|
4.5
|
13.5
|
0.5
|
OE2
|
J:GLU288
|
4.7
|
18.5
|
1.0
|
CD
|
J:GLU288
|
4.7
|
18.6
|
1.0
|
CE1
|
J:HIS136
|
4.8
|
18.9
|
1.0
|
CA
|
J:HIS528
|
4.9
|
15.0
|
1.0
|
|
Reference:
L.A.Varfolomeeva,
K.M.Polyakov,
A.S.Komolov,
T.V.Rakitina,
N.I.Dergousova,
P.V.Dorovatovskii,
K.M.Boyko,
T.V.Tikhonova,
V.O.Popov.
Improvement of Diffraction Properties of Thiocyanate Dehydrogenase Crystals To Be Published.
Page generated: Wed Jul 31 09:55:25 2024
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