Copper in PDB 3pxl: Type-2 Cu-Depleted Fungus Laccase From Trametes Hirsuta
Enzymatic activity of Type-2 Cu-Depleted Fungus Laccase From Trametes Hirsuta
All present enzymatic activity of Type-2 Cu-Depleted Fungus Laccase From Trametes Hirsuta:
1.10.3.2;
Protein crystallography data
The structure of Type-2 Cu-Depleted Fungus Laccase From Trametes Hirsuta, PDB code: 3pxl
was solved by
K.M.Polyakov,
T.V.Fedorova,
S.A.Kurzeev,
A.N.Popov,
V.S.Lamzin,
O.V.Koroleva,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
60.00 /
1.20
|
|
Space group
|
P 21 21 21
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
52.653,
77.051,
130.216,
90.00,
90.00,
90.00
|
|
R / Rfree (%)
|
15.3 /
17.9
|
Copper Binding Sites:
The binding sites of Copper atom in the Type-2 Cu-Depleted Fungus Laccase From Trametes Hirsuta
(pdb code 3pxl). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 5 binding sites of Copper where determined in the
Type-2 Cu-Depleted Fungus Laccase From Trametes Hirsuta, PDB code: 3pxl:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
Copper binding site 1 out
of 5 in 3pxl
Go back to
Copper Binding Sites List in 3pxl
Copper binding site 1 out
of 5 in the Type-2 Cu-Depleted Fungus Laccase From Trametes Hirsuta
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Type-2 Cu-Depleted Fungus Laccase From Trametes Hirsuta within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu1500
b:15.0
occ:0.75
|
CU
|
A:CU1500
|
0.0
|
15.0
|
0.8
|
|
CU
|
A:CU1500
|
1.7
|
27.4
|
0.1
|
|
NE2
|
A:HIS400
|
2.0
|
14.8
|
1.0
|
|
NE2
|
A:HIS452
|
2.0
|
16.7
|
1.0
|
|
NE2
|
A:HIS111
|
2.0
|
14.7
|
1.0
|
|
O
|
A:HOH1411
|
2.3
|
21.4
|
0.8
|
|
CE1
|
A:HIS400
|
2.8
|
14.8
|
1.0
|
|
CE1
|
A:HIS452
|
2.9
|
16.3
|
1.0
|
|
CE1
|
A:HIS111
|
2.9
|
14.8
|
1.0
|
|
HE1
|
A:HIS400
|
3.0
|
14.7
|
1.0
|
|
CD2
|
A:HIS452
|
3.0
|
15.2
|
1.0
|
|
CD2
|
A:HIS400
|
3.1
|
13.5
|
1.0
|
|
CD2
|
A:HIS111
|
3.1
|
13.6
|
1.0
|
|
HE1
|
A:HIS111
|
3.1
|
14.9
|
1.0
|
|
HE1
|
A:HIS452
|
3.1
|
15.7
|
1.0
|
|
HD2
|
A:HIS452
|
3.2
|
15.4
|
1.0
|
|
HD2
|
A:PHE450
|
3.3
|
14.8
|
1.0
|
|
HD2
|
A:HIS111
|
3.3
|
13.6
|
1.0
|
|
HD2
|
A:HIS400
|
3.4
|
13.5
|
1.0
|
|
HB3
|
A:PHE450
|
3.6
|
13.9
|
1.0
|
|
HG3
|
A:PRO79
|
3.7
|
14.5
|
1.0
|
|
ND1
|
A:HIS398
|
3.8
|
15.7
|
0.8
|
|
O
|
A:HOH867
|
3.8
|
26.4
|
1.0
|
|
ND1
|
A:HIS400
|
4.0
|
14.9
|
1.0
|
|
ND1
|
A:HIS452
|
4.0
|
14.8
|
1.0
|
|
CD2
|
A:PHE450
|
4.1
|
14.6
|
1.0
|
|
ND1
|
A:HIS111
|
4.1
|
15.5
|
1.0
|
|
CG
|
A:HIS452
|
4.1
|
15.7
|
1.0
|
|
CD2
|
A:HIS398
|
4.1
|
15.6
|
0.2
|
|
CG
|
A:HIS400
|
4.1
|
13.3
|
1.0
|
|
CG
|
A:HIS111
|
4.2
|
13.7
|
1.0
|
|
CE1
|
A:HIS398
|
4.4
|
13.3
|
0.8
|
|
HE1
|
A:HIS109
|
4.4
|
15.2
|
1.0
|
|
HG2
|
A:PRO79
|
4.4
|
14.6
|
1.0
|
|
HD2
|
A:HIS64
|
4.4
|
15.8
|
1.0
|
|
CB
|
A:PHE450
|
4.4
|
13.5
|
1.0
|
|
CG
|
A:PRO79
|
4.5
|
14.5
|
1.0
|
|
CU
|
A:CU1502
|
4.5
|
17.7
|
0.2
|
|
HD21
|
A:LEU459
|
4.5
|
17.1
|
0.0
|
|
HB2
|
A:PHE450
|
4.5
|
13.9
|
1.0
|
|
CD2
|
A:HIS64
|
4.6
|
15.9
|
1.0
|
|
CG
|
A:PHE450
|
4.7
|
13.8
|
1.0
|
|
NE2
|
A:HIS64
|
4.7
|
17.0
|
1.0
|
|
HD1
|
A:HIS400
|
4.7
|
14.3
|
1.0
|
|
HD2
|
A:HIS454
|
4.7
|
16.0
|
1.0
|
|
HE2
|
A:PHE450
|
4.8
|
15.6
|
1.0
|
|
HD1
|
A:HIS452
|
4.8
|
15.0
|
1.0
|
|
HD1
|
A:HIS111
|
4.8
|
14.9
|
1.0
|
|
HB3
|
A:PRO79
|
4.9
|
14.4
|
1.0
|
|
CE2
|
A:PHE450
|
4.9
|
16.4
|
1.0
|
|
CG
|
A:HIS398
|
4.9
|
14.9
|
0.8
|
|
HD22
|
A:LEU459
|
5.0
|
17.1
|
0.0
|
|
CD2
|
A:HIS454
|
5.0
|
16.0
|
1.0
|
|
CG
|
A:HIS398
|
5.0
|
15.1
|
0.2
|
|
Copper binding site 2 out
of 5 in 3pxl
Go back to
Copper Binding Sites List in 3pxl
Copper binding site 2 out
of 5 in the Type-2 Cu-Depleted Fungus Laccase From Trametes Hirsuta
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Type-2 Cu-Depleted Fungus Laccase From Trametes Hirsuta within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu1500
b:27.4
occ:0.15
|
CU
|
A:CU1500
|
0.0
|
27.4
|
0.1
|
|
CU
|
A:CU1500
|
1.7
|
15.0
|
0.8
|
|
O
|
A:HOH1411
|
1.8
|
21.4
|
0.8
|
|
ND1
|
A:HIS398
|
2.1
|
15.7
|
0.8
|
|
NE2
|
A:HIS400
|
2.3
|
14.8
|
1.0
|
|
NE2
|
A:HIS452
|
2.3
|
16.7
|
1.0
|
|
CD2
|
A:HIS398
|
2.6
|
15.6
|
0.2
|
|
CD2
|
A:HIS400
|
2.9
|
13.5
|
1.0
|
|
HD2
|
A:HIS400
|
2.9
|
13.5
|
1.0
|
|
CE1
|
A:HIS452
|
3.0
|
16.3
|
1.0
|
|
CE1
|
A:HIS398
|
3.0
|
13.3
|
0.8
|
|
HE1
|
A:HIS452
|
3.0
|
15.7
|
1.0
|
|
CG
|
A:HIS398
|
3.2
|
14.9
|
0.8
|
|
CD2
|
A:HIS452
|
3.3
|
15.2
|
1.0
|
|
HD2
|
A:HIS454
|
3.3
|
16.0
|
1.0
|
|
CG
|
A:HIS398
|
3.3
|
15.1
|
0.2
|
|
CE1
|
A:HIS400
|
3.4
|
14.8
|
1.0
|
|
NE2
|
A:HIS111
|
3.5
|
14.7
|
1.0
|
|
CU
|
A:CU1502
|
3.6
|
17.7
|
0.2
|
|
HD2
|
A:HIS452
|
3.6
|
15.4
|
1.0
|
|
NE2
|
A:HIS398
|
3.7
|
14.7
|
0.2
|
|
CB
|
A:HIS398
|
3.7
|
15.4
|
1.0
|
|
HE1
|
A:HIS400
|
3.7
|
14.7
|
1.0
|
|
CD2
|
A:HIS454
|
3.8
|
16.0
|
1.0
|
|
ND1
|
A:HIS452
|
4.1
|
14.8
|
1.0
|
|
NE2
|
A:HIS454
|
4.1
|
15.5
|
1.0
|
|
CG
|
A:HIS400
|
4.1
|
13.3
|
1.0
|
|
NE2
|
A:HIS398
|
4.2
|
19.4
|
0.8
|
|
O
|
A:HOH867
|
4.2
|
26.4
|
1.0
|
|
HD2
|
A:HIS64
|
4.2
|
15.8
|
1.0
|
|
HD2
|
A:HIS111
|
4.3
|
13.6
|
1.0
|
|
CD2
|
A:HIS398
|
4.3
|
14.8
|
0.8
|
|
CG
|
A:HIS452
|
4.3
|
15.7
|
1.0
|
|
ND1
|
A:HIS400
|
4.3
|
14.9
|
1.0
|
|
CD2
|
A:HIS111
|
4.3
|
13.6
|
1.0
|
|
HB3
|
A:PHE450
|
4.4
|
13.9
|
1.0
|
|
NE2
|
A:HIS64
|
4.4
|
17.0
|
1.0
|
|
CU
|
A:CU1501
|
4.4
|
16.1
|
0.8
|
|
CD2
|
A:HIS64
|
4.5
|
15.9
|
1.0
|
|
HE1
|
A:HIS66
|
4.5
|
15.2
|
1.0
|
|
ND1
|
A:HIS398
|
4.5
|
14.7
|
0.2
|
|
CE1
|
A:HIS111
|
4.5
|
14.8
|
1.0
|
|
O
|
A:HIS398
|
4.6
|
13.7
|
1.0
|
|
HE1
|
A:HIS109
|
4.6
|
15.2
|
1.0
|
|
CE1
|
A:HIS398
|
4.7
|
13.2
|
0.2
|
|
HE1
|
A:HIS111
|
4.7
|
14.9
|
1.0
|
|
HD2
|
A:PHE450
|
4.8
|
14.8
|
1.0
|
|
HD1
|
A:HIS452
|
4.8
|
15.0
|
1.0
|
|
CG
|
A:HIS454
|
4.8
|
15.9
|
1.0
|
|
ND1
|
A:HIS66
|
4.9
|
15.7
|
1.0
|
|
C
|
A:HIS398
|
4.9
|
13.8
|
1.0
|
|
CE1
|
A:HIS66
|
4.9
|
15.4
|
1.0
|
|
CA
|
A:HIS398
|
4.9
|
14.4
|
1.0
|
|
Copper binding site 3 out
of 5 in 3pxl
Go back to
Copper Binding Sites List in 3pxl
Copper binding site 3 out
of 5 in the Type-2 Cu-Depleted Fungus Laccase From Trametes Hirsuta
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Type-2 Cu-Depleted Fungus Laccase From Trametes Hirsuta within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu1501
b:16.1
occ:0.80
|
ND1
|
A:HIS66
|
2.0
|
15.7
|
1.0
|
|
NE2
|
A:HIS109
|
2.0
|
15.9
|
1.0
|
|
NE2
|
A:HIS454
|
2.1
|
15.5
|
1.0
|
|
HD2
|
A:HIS64
|
2.8
|
15.8
|
1.0
|
|
CE1
|
A:HIS66
|
2.9
|
15.4
|
1.0
|
|
HB2
|
A:HIS66
|
2.9
|
13.3
|
1.0
|
|
O
|
A:HOH1411
|
3.0
|
21.4
|
0.8
|
|
CE1
|
A:HIS109
|
3.0
|
15.7
|
1.0
|
|
CE1
|
A:HIS454
|
3.0
|
15.6
|
1.0
|
|
CD2
|
A:HIS109
|
3.0
|
15.1
|
1.0
|
|
HE1
|
A:HIS66
|
3.0
|
15.2
|
1.0
|
|
CG
|
A:HIS66
|
3.0
|
13.6
|
1.0
|
|
HE1
|
A:HIS454
|
3.1
|
15.2
|
1.0
|
|
HE1
|
A:HIS109
|
3.2
|
15.2
|
1.0
|
|
CD2
|
A:HIS454
|
3.2
|
16.0
|
1.0
|
|
HD2
|
A:HIS109
|
3.2
|
14.9
|
1.0
|
|
HZ2
|
A:TRP107
|
3.3
|
13.7
|
1.0
|
|
HD2
|
A:HIS454
|
3.4
|
16.0
|
1.0
|
|
CB
|
A:HIS66
|
3.5
|
13.7
|
1.0
|
|
CZ2
|
A:TRP107
|
3.6
|
14.1
|
1.0
|
|
CD2
|
A:HIS64
|
3.7
|
15.9
|
1.0
|
|
HB2
|
A:ALA241
|
3.7
|
14.6
|
0.0
|
|
HE1
|
A:TRP107
|
3.8
|
13.9
|
1.0
|
|
CE2
|
A:TRP107
|
3.8
|
13.1
|
1.0
|
|
NE1
|
A:TRP107
|
4.0
|
14.6
|
1.0
|
|
HB1
|
A:ALA241
|
4.0
|
14.6
|
0.0
|
|
NE2
|
A:HIS66
|
4.0
|
15.9
|
1.0
|
|
HB3
|
A:HIS66
|
4.0
|
13.3
|
1.0
|
|
ND1
|
A:HIS109
|
4.1
|
14.8
|
1.0
|
|
CU
|
A:CU1502
|
4.1
|
17.7
|
0.2
|
|
CD2
|
A:HIS66
|
4.1
|
15.6
|
1.0
|
|
CG
|
A:HIS109
|
4.1
|
14.4
|
1.0
|
|
ND1
|
A:HIS454
|
4.1
|
14.3
|
1.0
|
|
NE2
|
A:HIS64
|
4.2
|
17.0
|
1.0
|
|
ND1
|
A:HIS398
|
4.2
|
15.7
|
0.8
|
|
CE1
|
A:HIS398
|
4.3
|
13.3
|
0.8
|
|
CG
|
A:HIS454
|
4.3
|
15.9
|
1.0
|
|
CB
|
A:ALA241
|
4.3
|
14.2
|
1.0
|
|
CH2
|
A:TRP107
|
4.3
|
13.8
|
1.0
|
|
CU
|
A:CU1500
|
4.4
|
27.4
|
0.1
|
|
HA
|
A:HIS66
|
4.4
|
13.7
|
1.0
|
|
O
|
A:HOH867
|
4.5
|
26.4
|
1.0
|
|
HH2
|
A:TRP107
|
4.5
|
13.8
|
1.0
|
|
CA
|
A:HIS66
|
4.6
|
13.3
|
1.0
|
|
HD2
|
A:HIS111
|
4.7
|
13.6
|
1.0
|
|
CD2
|
A:TRP107
|
4.7
|
13.9
|
1.0
|
|
HE2
|
A:HIS66
|
4.8
|
15.8
|
1.0
|
|
CG
|
A:HIS64
|
4.9
|
15.4
|
1.0
|
|
HD1
|
A:HIS109
|
4.9
|
14.6
|
1.0
|
|
CD1
|
A:TRP107
|
4.9
|
13.8
|
1.0
|
|
CD2
|
A:HIS398
|
4.9
|
15.6
|
0.2
|
|
HD1
|
A:HIS454
|
4.9
|
14.6
|
1.0
|
|
HB3
|
A:ALA241
|
4.9
|
14.6
|
0.0
|
|
HB3
|
A:HIS64
|
4.9
|
13.6
|
1.0
|
|
HD2
|
A:HIS66
|
5.0
|
15.3
|
1.0
|
|
Copper binding site 4 out
of 5 in 3pxl
Go back to
Copper Binding Sites List in 3pxl
Copper binding site 4 out
of 5 in the Type-2 Cu-Depleted Fungus Laccase From Trametes Hirsuta
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of Type-2 Cu-Depleted Fungus Laccase From Trametes Hirsuta within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu1503
b:14.6
occ:0.80
|
ND1
|
A:HIS458
|
2.0
|
17.9
|
1.0
|
|
ND1
|
A:HIS395
|
2.0
|
14.8
|
1.0
|
|
SG
|
A:CYS453
|
2.2
|
16.5
|
1.0
|
|
HD13
|
A:ILE455
|
2.7
|
17.4
|
0.0
|
|
CE1
|
A:HIS458
|
3.0
|
15.9
|
1.0
|
|
CE1
|
A:HIS395
|
3.0
|
16.1
|
1.0
|
|
HB
|
A:ILE455
|
3.0
|
14.7
|
1.0
|
|
CG
|
A:HIS458
|
3.0
|
15.1
|
1.0
|
|
HD2
|
A:PHE463
|
3.0
|
14.6
|
1.0
|
|
HB3
|
A:HIS395
|
3.1
|
15.2
|
1.0
|
|
CG
|
A:HIS395
|
3.1
|
15.3
|
1.0
|
|
HE1
|
A:HIS458
|
3.1
|
16.2
|
1.0
|
|
HE1
|
A:HIS395
|
3.1
|
16.3
|
1.0
|
|
HB2
|
A:HIS458
|
3.2
|
14.9
|
1.0
|
|
HG
|
A:CYS453
|
3.3
|
15.8
|
1.0
|
|
CB
|
A:CYS453
|
3.3
|
13.9
|
1.0
|
|
HB3
|
A:HIS458
|
3.3
|
14.9
|
1.0
|
|
HA
|
A:HIS395
|
3.3
|
15.3
|
1.0
|
|
HE2
|
A:PHE463
|
3.3
|
14.9
|
1.0
|
|
HB2
|
A:CYS453
|
3.4
|
14.2
|
1.0
|
|
CB
|
A:HIS458
|
3.4
|
15.1
|
1.0
|
|
HB3
|
A:CYS453
|
3.4
|
14.2
|
1.0
|
|
CB
|
A:HIS395
|
3.5
|
14.7
|
1.0
|
|
CD1
|
A:ILE455
|
3.6
|
17.3
|
1.0
|
|
CD2
|
A:PHE463
|
3.8
|
14.7
|
1.0
|
|
HD2
|
A:PRO396
|
3.8
|
14.6
|
1.0
|
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CB
|
A:ILE455
|
3.9
|
14.6
|
1.0
|
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CE2
|
A:PHE463
|
3.9
|
15.2
|
1.0
|
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HD12
|
A:ILE455
|
3.9
|
17.4
|
0.0
|
|
CA
|
A:HIS395
|
3.9
|
15.4
|
1.0
|
|
CG1
|
A:ILE455
|
4.0
|
15.1
|
1.0
|
|
HG13
|
A:ILE455
|
4.1
|
15.1
|
1.0
|
|
H
|
A:ILE455
|
4.1
|
15.1
|
1.0
|
|
NE2
|
A:HIS458
|
4.1
|
16.0
|
1.0
|
|
NE2
|
A:HIS395
|
4.1
|
17.8
|
1.0
|
|
CD2
|
A:HIS458
|
4.2
|
15.3
|
1.0
|
|
CD2
|
A:HIS395
|
4.2
|
17.1
|
1.0
|
|
HD11
|
A:ILE455
|
4.2
|
17.4
|
0.0
|
|
HG22
|
A:ILE455
|
4.4
|
15.0
|
0.0
|
|
HB2
|
A:HIS395
|
4.4
|
15.1
|
1.0
|
|
O
|
A:GLY392
|
4.6
|
22.3
|
1.0
|
|
CG2
|
A:ILE455
|
4.6
|
15.2
|
1.0
|
|
CA
|
A:CYS453
|
4.6
|
14.2
|
1.0
|
|
CD
|
A:PRO396
|
4.7
|
15.2
|
1.0
|
|
N
|
A:ILE455
|
4.8
|
14.6
|
1.0
|
|
HA
|
A:CYS453
|
4.8
|
14.0
|
1.0
|
|
HG21
|
A:ILE455
|
4.8
|
15.0
|
0.0
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HD3
|
A:PRO396
|
4.8
|
14.4
|
1.0
|
|
HE2
|
A:HIS458
|
4.9
|
15.8
|
1.0
|
|
HE2
|
A:HIS395
|
4.9
|
17.0
|
1.0
|
|
CA
|
A:ILE455
|
4.9
|
14.8
|
1.0
|
|
CA
|
A:HIS458
|
4.9
|
15.0
|
1.0
|
|
HE1
|
A:PHE397
|
4.9
|
15.9
|
1.0
|
|
C
|
A:HIS395
|
4.9
|
15.4
|
1.0
|
|
N
|
A:HIS395
|
5.0
|
15.7
|
1.0
|
|
HZ
|
A:PHE337
|
5.0
|
17.8
|
1.0
|
|
O
|
A:ILE455
|
5.0
|
14.9
|
1.0
|
|
HG12
|
A:ILE455
|
5.0
|
15.4
|
1.0
|
|
Copper binding site 5 out
of 5 in 3pxl
Go back to
Copper Binding Sites List in 3pxl
Copper binding site 5 out
of 5 in the Type-2 Cu-Depleted Fungus Laccase From Trametes Hirsuta
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 5 of Type-2 Cu-Depleted Fungus Laccase From Trametes Hirsuta within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu1502
b:17.7
occ:0.20
|
CE1
|
A:HIS398
|
1.4
|
13.3
|
0.8
|
|
NE2
|
A:HIS64
|
1.9
|
17.0
|
1.0
|
|
NE2
|
A:HIS398
|
2.0
|
14.7
|
0.2
|
|
NE2
|
A:HIS398
|
2.3
|
19.4
|
0.8
|
|
ND1
|
A:HIS398
|
2.6
|
15.7
|
0.8
|
|
CD2
|
A:HIS398
|
2.6
|
15.6
|
0.2
|
|
O
|
A:HOH1003
|
2.6
|
17.4
|
1.0
|
|
CE1
|
A:HIS64
|
2.8
|
15.6
|
1.0
|
|
CD2
|
A:HIS64
|
2.9
|
15.9
|
1.0
|
|
CE1
|
A:HIS398
|
2.9
|
13.2
|
0.2
|
|
HE1
|
A:HIS64
|
3.0
|
16.0
|
1.0
|
|
HA
|
A:HIS66
|
3.0
|
13.7
|
1.0
|
|
HD2
|
A:HIS64
|
3.1
|
15.8
|
1.0
|
|
ND1
|
A:HIS66
|
3.3
|
15.7
|
1.0
|
|
H
|
A:GLY67
|
3.4
|
14.2
|
1.0
|
|
NE2
|
A:HIS400
|
3.5
|
14.8
|
1.0
|
|
CE1
|
A:HIS400
|
3.5
|
14.8
|
1.0
|
|
CD2
|
A:HIS398
|
3.5
|
14.8
|
0.8
|
|
CU
|
A:CU1500
|
3.6
|
27.4
|
0.1
|
|
CG
|
A:HIS66
|
3.6
|
13.6
|
1.0
|
|
CG
|
A:HIS398
|
3.6
|
14.9
|
0.8
|
|
CE1
|
A:HIS66
|
3.7
|
15.4
|
1.0
|
|
CD2
|
A:HIS400
|
3.7
|
13.5
|
1.0
|
|
CG
|
A:HIS398
|
3.7
|
15.1
|
0.2
|
|
ND1
|
A:HIS400
|
3.7
|
14.9
|
1.0
|
|
O
|
A:HOH1411
|
3.7
|
21.4
|
0.8
|
|
HA
|
A:HIS400
|
3.8
|
13.3
|
1.0
|
|
HE1
|
A:HIS400
|
3.8
|
14.7
|
1.0
|
|
CG
|
A:HIS400
|
3.8
|
13.3
|
1.0
|
|
ND1
|
A:HIS398
|
3.8
|
14.7
|
0.2
|
|
ND1
|
A:HIS64
|
3.9
|
16.0
|
1.0
|
|
CA
|
A:HIS66
|
3.9
|
13.3
|
1.0
|
|
HE1
|
A:HIS66
|
4.0
|
15.2
|
1.0
|
|
CG
|
A:HIS64
|
4.0
|
15.4
|
1.0
|
|
NE2
|
A:HIS66
|
4.0
|
15.9
|
1.0
|
|
CD2
|
A:HIS66
|
4.0
|
15.6
|
1.0
|
|
N
|
A:GLY67
|
4.1
|
14.2
|
1.0
|
|
CU
|
A:CU1501
|
4.1
|
16.1
|
0.8
|
|
HD2
|
A:HIS400
|
4.1
|
13.5
|
1.0
|
|
HD1
|
A:HIS400
|
4.1
|
14.3
|
1.0
|
|
CB
|
A:HIS66
|
4.1
|
13.7
|
1.0
|
|
HB2
|
A:HIS66
|
4.2
|
13.3
|
1.0
|
|
C
|
A:HIS66
|
4.5
|
13.9
|
1.0
|
|
CU
|
A:CU1500
|
4.5
|
15.0
|
0.8
|
|
O
|
A:HOH1038
|
4.5
|
15.5
|
1.0
|
|
HE2
|
A:HIS66
|
4.6
|
15.8
|
1.0
|
|
CA
|
A:HIS400
|
4.6
|
13.3
|
1.0
|
|
HD2
|
A:HIS66
|
4.6
|
15.3
|
1.0
|
|
HD1
|
A:HIS64
|
4.7
|
15.6
|
1.0
|
|
O
|
A:HOH1089
|
4.7
|
19.6
|
1.0
|
|
CB
|
A:HIS400
|
4.7
|
13.6
|
1.0
|
|
HA2
|
A:GLY67
|
4.9
|
14.6
|
1.0
|
|
HD2
|
A:HIS454
|
4.9
|
16.0
|
1.0
|
|
HB3
|
A:HIS400
|
4.9
|
13.2
|
1.0
|
|
N
|
A:HIS66
|
5.0
|
14.4
|
1.0
|
|
Reference:
K.M.Polyakov,
T.V.Fedorova,
S.A.Kurzeev,
A.N.Popov,
V.S.Lamzin,
O.V.Koroleva.
Crystal Structure of T2-Depleted Fungal Laccase From Trametes Hirsuta at Low and High Dose of Ionization Radiation. To Be Published.
Page generated: Sun Dec 13 11:11:21 2020
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