Copper in PDB 5or3: Crystal Structure of Aspergillus Oryzae Catechol Oxidase in Met/Deoxy- Form
Protein crystallography data
The structure of Crystal Structure of Aspergillus Oryzae Catechol Oxidase in Met/Deoxy- Form, PDB code: 5or3
was solved by
N.Hakulinen,
L.Penttinen,
C.Rutanen,
J.Rouvinen,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
29.12 /
1.80
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
60.627,
81.392,
82.200,
87.19,
89.23,
73.89
|
R / Rfree (%)
|
17.6 /
20.7
|
Copper Binding Sites:
The binding sites of Copper atom in the Crystal Structure of Aspergillus Oryzae Catechol Oxidase in Met/Deoxy- Form
(pdb code 5or3). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 8 binding sites of Copper where determined in the
Crystal Structure of Aspergillus Oryzae Catechol Oxidase in Met/Deoxy- Form, PDB code: 5or3:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Copper binding site 1 out
of 8 in 5or3
Go back to
Copper Binding Sites List in 5or3
Copper binding site 1 out
of 8 in the Crystal Structure of Aspergillus Oryzae Catechol Oxidase in Met/Deoxy- Form
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Crystal Structure of Aspergillus Oryzae Catechol Oxidase in Met/Deoxy- Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu2001
b:31.4
occ:1.00
|
NE2
|
A:HIS102
|
2.0
|
20.5
|
1.0
|
NE2
|
A:HIS119
|
2.0
|
20.8
|
1.0
|
NE2
|
A:HIS110
|
2.2
|
24.3
|
1.0
|
O
|
A:HOH2323
|
2.4
|
28.8
|
1.0
|
HE1
|
A:HIS110
|
2.7
|
28.8
|
1.0
|
CE1
|
A:HIS110
|
2.8
|
24.0
|
1.0
|
CE1
|
A:HIS119
|
2.9
|
22.0
|
1.0
|
CE1
|
A:HIS102
|
2.9
|
20.5
|
1.0
|
HE1
|
A:HIS119
|
3.0
|
26.4
|
1.0
|
CD2
|
A:HIS102
|
3.0
|
19.1
|
1.0
|
HE1
|
A:HIS102
|
3.1
|
24.6
|
1.0
|
CD2
|
A:HIS119
|
3.2
|
20.6
|
1.0
|
HD2
|
A:HIS102
|
3.2
|
22.9
|
1.0
|
HD2
|
A:HIS119
|
3.4
|
24.7
|
1.0
|
CD2
|
A:HIS110
|
3.4
|
24.1
|
1.0
|
HE2
|
A:PHE308
|
3.8
|
21.9
|
1.0
|
HZ
|
A:PHE308
|
3.8
|
21.8
|
1.0
|
HD2
|
A:HIS110
|
3.8
|
28.9
|
1.0
|
HD12
|
A:ILE109
|
3.9
|
23.1
|
1.0
|
HG13
|
A:ILE109
|
3.9
|
27.3
|
1.0
|
ND1
|
A:HIS110
|
4.0
|
26.1
|
1.0
|
HD11
|
A:ILE109
|
4.0
|
23.1
|
1.0
|
O
|
A:HOH2296
|
4.0
|
24.4
|
1.0
|
ND1
|
A:HIS102
|
4.1
|
19.3
|
1.0
|
ND1
|
A:HIS119
|
4.1
|
18.5
|
1.0
|
HZ3
|
A:TRP118
|
4.1
|
19.6
|
1.0
|
CG
|
A:HIS102
|
4.1
|
17.6
|
1.0
|
CG
|
A:HIS119
|
4.2
|
17.4
|
1.0
|
CG
|
A:HIS110
|
4.3
|
24.0
|
1.0
|
CU
|
A:CU2002
|
4.3
|
28.1
|
1.0
|
CD1
|
A:ILE109
|
4.3
|
19.2
|
1.0
|
CE2
|
A:PHE308
|
4.5
|
18.2
|
1.0
|
CZ
|
A:PHE308
|
4.5
|
18.1
|
1.0
|
HE1
|
A:PHE115
|
4.5
|
22.3
|
1.0
|
HD1
|
A:HIS110
|
4.6
|
31.3
|
1.0
|
CG1
|
A:ILE109
|
4.6
|
22.7
|
1.0
|
CZ3
|
A:TRP118
|
4.6
|
16.3
|
1.0
|
NE2
|
A:HIS312
|
4.7
|
19.1
|
1.0
|
HE1
|
A:HIS312
|
4.7
|
22.4
|
1.0
|
HD1
|
A:HIS119
|
4.8
|
22.2
|
1.0
|
HD1
|
A:HIS102
|
4.8
|
23.2
|
1.0
|
HE3
|
A:TRP118
|
4.9
|
18.4
|
1.0
|
CE1
|
A:HIS312
|
4.9
|
18.6
|
1.0
|
HG
|
A:SER302
|
5.0
|
32.8
|
1.0
|
|
Copper binding site 2 out
of 8 in 5or3
Go back to
Copper Binding Sites List in 5or3
Copper binding site 2 out
of 8 in the Crystal Structure of Aspergillus Oryzae Catechol Oxidase in Met/Deoxy- Form
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Crystal Structure of Aspergillus Oryzae Catechol Oxidase in Met/Deoxy- Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu2002
b:28.1
occ:1.00
|
NE2
|
A:HIS312
|
2.0
|
19.1
|
1.0
|
NE2
|
A:HIS284
|
2.1
|
18.4
|
1.0
|
NE2
|
A:HIS288
|
2.1
|
20.5
|
1.0
|
O
|
A:HOH2323
|
2.2
|
28.8
|
1.0
|
CE1
|
A:HIS312
|
2.6
|
18.6
|
1.0
|
HE1
|
A:HIS312
|
2.6
|
22.4
|
1.0
|
CD2
|
A:HIS284
|
3.0
|
18.9
|
1.0
|
CD2
|
A:HIS288
|
3.0
|
22.7
|
1.0
|
CE1
|
A:HIS284
|
3.0
|
20.9
|
1.0
|
CE1
|
A:HIS288
|
3.1
|
22.3
|
1.0
|
HD2
|
A:HIS288
|
3.1
|
27.2
|
1.0
|
HD2
|
A:HIS284
|
3.1
|
22.7
|
1.0
|
CD2
|
A:HIS312
|
3.2
|
17.3
|
1.0
|
HE1
|
A:HIS284
|
3.3
|
25.1
|
1.0
|
HE1
|
A:HIS288
|
3.3
|
26.8
|
1.0
|
HD2
|
A:HIS312
|
3.6
|
20.7
|
1.0
|
HE2
|
A:PHE308
|
3.6
|
21.9
|
1.0
|
HD2
|
A:HIS311
|
3.7
|
20.2
|
1.0
|
ND1
|
A:HIS312
|
3.9
|
18.0
|
1.0
|
O
|
A:HOH2296
|
3.9
|
24.4
|
1.0
|
HE2
|
A:HIS311
|
4.0
|
20.4
|
1.0
|
HE1
|
A:PHE115
|
4.1
|
22.3
|
1.0
|
ND1
|
A:HIS284
|
4.1
|
18.8
|
1.0
|
CG
|
A:HIS284
|
4.1
|
17.7
|
1.0
|
CG
|
A:HIS312
|
4.2
|
16.4
|
1.0
|
CG
|
A:HIS288
|
4.2
|
21.0
|
1.0
|
CE2
|
A:PHE308
|
4.2
|
18.2
|
1.0
|
ND1
|
A:HIS288
|
4.2
|
23.8
|
1.0
|
CD2
|
A:HIS311
|
4.3
|
16.9
|
1.0
|
CU
|
A:CU2001
|
4.3
|
31.4
|
1.0
|
NE2
|
A:HIS311
|
4.4
|
17.0
|
1.0
|
HD2
|
A:HIS119
|
4.4
|
24.7
|
1.0
|
NE2
|
A:HIS119
|
4.5
|
20.8
|
1.0
|
HD1
|
A:HIS312
|
4.6
|
21.6
|
1.0
|
CD2
|
A:HIS119
|
4.6
|
20.6
|
1.0
|
HZ
|
A:PHE115
|
4.7
|
22.9
|
1.0
|
HD2
|
A:HIS110
|
4.7
|
28.9
|
1.0
|
HG13
|
A:ILE315
|
4.7
|
19.7
|
1.0
|
HZ
|
A:PHE308
|
4.8
|
21.8
|
1.0
|
NE2
|
A:HIS110
|
4.8
|
24.3
|
1.0
|
HD2
|
A:PHE308
|
4.8
|
21.4
|
1.0
|
CZ
|
A:PHE308
|
4.8
|
18.1
|
1.0
|
CD2
|
A:PHE308
|
4.8
|
17.8
|
1.0
|
HD1
|
A:HIS284
|
4.9
|
22.6
|
1.0
|
CE1
|
A:PHE115
|
4.9
|
18.6
|
1.0
|
HG
|
A:SER302
|
5.0
|
32.8
|
1.0
|
HD1
|
A:HIS288
|
5.0
|
28.5
|
1.0
|
|
Copper binding site 3 out
of 8 in 5or3
Go back to
Copper Binding Sites List in 5or3
Copper binding site 3 out
of 8 in the Crystal Structure of Aspergillus Oryzae Catechol Oxidase in Met/Deoxy- Form
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Crystal Structure of Aspergillus Oryzae Catechol Oxidase in Met/Deoxy- Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu2001
b:24.9
occ:1.00
|
NE2
|
B:HIS119
|
2.0
|
18.0
|
1.0
|
NE2
|
B:HIS102
|
2.1
|
17.6
|
1.0
|
NE2
|
B:HIS110
|
2.2
|
24.4
|
1.0
|
O
|
B:HOH2292
|
2.2
|
25.6
|
1.0
|
HE1
|
B:HIS110
|
2.7
|
27.0
|
1.0
|
CE1
|
B:HIS110
|
2.7
|
22.5
|
1.0
|
CE1
|
B:HIS119
|
2.8
|
18.4
|
1.0
|
HE1
|
B:HIS119
|
2.9
|
22.1
|
1.0
|
CE1
|
B:HIS102
|
3.0
|
18.0
|
1.0
|
CD2
|
B:HIS102
|
3.0
|
17.0
|
1.0
|
CD2
|
B:HIS119
|
3.1
|
15.9
|
1.0
|
HD2
|
B:HIS102
|
3.2
|
20.5
|
1.0
|
HE1
|
B:HIS102
|
3.2
|
21.6
|
1.0
|
CD2
|
B:HIS110
|
3.4
|
23.4
|
1.0
|
HD2
|
B:HIS119
|
3.4
|
19.1
|
1.0
|
HD12
|
B:ILE109
|
3.7
|
21.0
|
1.0
|
HD11
|
B:ILE109
|
3.7
|
21.0
|
1.0
|
HD2
|
B:HIS110
|
3.8
|
28.0
|
1.0
|
HE2
|
B:PHE308
|
3.8
|
21.0
|
1.0
|
HZ
|
B:PHE308
|
3.8
|
19.1
|
1.0
|
HG13
|
B:ILE109
|
3.8
|
22.9
|
1.0
|
ND1
|
B:HIS110
|
3.9
|
22.6
|
1.0
|
O
|
B:HOH2249
|
4.0
|
22.2
|
1.0
|
ND1
|
B:HIS119
|
4.0
|
15.7
|
1.0
|
CD1
|
B:ILE109
|
4.1
|
17.5
|
1.0
|
ND1
|
B:HIS102
|
4.1
|
16.3
|
1.0
|
HZ3
|
B:TRP118
|
4.2
|
17.9
|
1.0
|
CG
|
B:HIS102
|
4.2
|
15.8
|
1.0
|
CG
|
B:HIS119
|
4.2
|
15.2
|
1.0
|
CG
|
B:HIS110
|
4.2
|
22.9
|
1.0
|
CU
|
B:CU2002
|
4.4
|
25.3
|
1.0
|
HE1
|
B:PHE115
|
4.4
|
21.9
|
1.0
|
CE2
|
B:PHE308
|
4.5
|
17.5
|
1.0
|
CZ
|
B:PHE308
|
4.5
|
15.9
|
1.0
|
CG1
|
B:ILE109
|
4.5
|
19.1
|
1.0
|
HD1
|
B:HIS110
|
4.6
|
27.2
|
1.0
|
NE2
|
B:HIS312
|
4.7
|
17.0
|
1.0
|
CZ3
|
B:TRP118
|
4.7
|
14.9
|
1.0
|
HE1
|
B:HIS312
|
4.8
|
19.9
|
1.0
|
HD1
|
B:HIS119
|
4.8
|
18.9
|
1.0
|
HD1
|
B:PHE115
|
4.9
|
20.7
|
1.0
|
HE3
|
B:TRP118
|
4.9
|
17.9
|
1.0
|
HD1
|
B:HIS102
|
4.9
|
19.6
|
1.0
|
CE1
|
B:HIS312
|
4.9
|
16.6
|
1.0
|
|
Copper binding site 4 out
of 8 in 5or3
Go back to
Copper Binding Sites List in 5or3
Copper binding site 4 out
of 8 in the Crystal Structure of Aspergillus Oryzae Catechol Oxidase in Met/Deoxy- Form
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of Crystal Structure of Aspergillus Oryzae Catechol Oxidase in Met/Deoxy- Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu2002
b:25.3
occ:1.00
|
NE2
|
B:HIS288
|
1.9
|
21.0
|
1.0
|
NE2
|
B:HIS312
|
2.0
|
17.0
|
1.0
|
NE2
|
B:HIS284
|
2.1
|
19.4
|
1.0
|
O
|
B:HOH2292
|
2.4
|
25.6
|
1.0
|
CE1
|
B:HIS312
|
2.8
|
16.6
|
1.0
|
HE1
|
B:HIS312
|
2.9
|
19.9
|
1.0
|
CE1
|
B:HIS288
|
2.9
|
22.1
|
1.0
|
CD2
|
B:HIS288
|
3.0
|
21.7
|
1.0
|
CE1
|
B:HIS284
|
3.0
|
22.5
|
1.0
|
HE1
|
B:HIS288
|
3.1
|
26.6
|
1.0
|
CD2
|
B:HIS284
|
3.1
|
20.4
|
1.0
|
CD2
|
B:HIS312
|
3.1
|
17.0
|
1.0
|
HD2
|
B:HIS288
|
3.2
|
26.1
|
1.0
|
HE1
|
B:HIS284
|
3.2
|
27.0
|
1.0
|
HD2
|
B:HIS284
|
3.3
|
24.5
|
1.0
|
HD2
|
B:HIS312
|
3.4
|
20.5
|
1.0
|
HE2
|
B:PHE308
|
3.5
|
21.0
|
1.0
|
HD2
|
B:HIS311
|
3.5
|
22.3
|
1.0
|
HE2
|
B:HIS311
|
3.9
|
23.1
|
1.0
|
ND1
|
B:HIS312
|
4.0
|
17.1
|
1.0
|
O
|
B:HOH2249
|
4.0
|
22.2
|
1.0
|
ND1
|
B:HIS288
|
4.0
|
24.2
|
1.0
|
CE2
|
B:PHE308
|
4.0
|
17.5
|
1.0
|
CG
|
B:HIS288
|
4.1
|
22.0
|
1.0
|
ND1
|
B:HIS284
|
4.1
|
21.2
|
1.0
|
HE1
|
B:PHE115
|
4.1
|
21.9
|
1.0
|
CG
|
B:HIS312
|
4.1
|
15.5
|
1.0
|
CD2
|
B:HIS311
|
4.2
|
18.6
|
1.0
|
CG
|
B:HIS284
|
4.2
|
19.7
|
1.0
|
NE2
|
B:HIS311
|
4.3
|
19.2
|
1.0
|
CU
|
B:CU2001
|
4.4
|
24.9
|
1.0
|
HD2
|
B:HIS119
|
4.4
|
19.1
|
1.0
|
NE2
|
B:HIS119
|
4.6
|
18.0
|
1.0
|
HZ
|
B:PHE308
|
4.6
|
19.1
|
1.0
|
HD2
|
B:PHE308
|
4.6
|
20.5
|
1.0
|
CD2
|
B:HIS119
|
4.6
|
15.9
|
1.0
|
CZ
|
B:PHE308
|
4.7
|
15.9
|
1.0
|
CD2
|
B:PHE308
|
4.7
|
17.0
|
1.0
|
HD1
|
B:HIS312
|
4.7
|
20.6
|
1.0
|
HZ
|
B:PHE115
|
4.7
|
20.5
|
1.0
|
HG13
|
B:ILE315
|
4.8
|
19.3
|
1.0
|
HD1
|
B:HIS288
|
4.8
|
29.0
|
1.0
|
NE2
|
B:HIS110
|
4.8
|
24.4
|
1.0
|
HD2
|
B:HIS110
|
4.8
|
28.0
|
1.0
|
HD1
|
B:HIS284
|
4.9
|
25.5
|
1.0
|
HG
|
B:SER302
|
4.9
|
24.3
|
1.0
|
OG
|
B:SER302
|
4.9
|
20.2
|
1.0
|
CE1
|
B:PHE115
|
5.0
|
18.2
|
1.0
|
|
Copper binding site 5 out
of 8 in 5or3
Go back to
Copper Binding Sites List in 5or3
Copper binding site 5 out
of 8 in the Crystal Structure of Aspergillus Oryzae Catechol Oxidase in Met/Deoxy- Form
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 5 of Crystal Structure of Aspergillus Oryzae Catechol Oxidase in Met/Deoxy- Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cu2001
b:27.2
occ:1.00
|
NE2
|
C:HIS119
|
2.0
|
24.3
|
1.0
|
NE2
|
C:HIS102
|
2.0
|
24.0
|
1.0
|
NE2
|
C:HIS110
|
2.2
|
28.3
|
1.0
|
O2
|
C:PER2009
|
2.2
|
30.1
|
1.0
|
O1
|
C:PER2009
|
2.6
|
37.9
|
1.0
|
CE1
|
C:HIS110
|
2.9
|
28.0
|
1.0
|
CE1
|
C:HIS119
|
2.9
|
25.6
|
1.0
|
HE1
|
C:HIS110
|
2.9
|
33.6
|
1.0
|
CE1
|
C:HIS102
|
2.9
|
23.9
|
1.0
|
CD2
|
C:HIS102
|
3.0
|
22.9
|
1.0
|
HE1
|
C:HIS119
|
3.0
|
30.7
|
1.0
|
CD2
|
C:HIS119
|
3.0
|
24.8
|
1.0
|
HE1
|
C:HIS102
|
3.1
|
28.7
|
1.0
|
HD2
|
C:HIS102
|
3.2
|
27.5
|
1.0
|
HD2
|
C:HIS119
|
3.3
|
29.8
|
1.0
|
CD2
|
C:HIS110
|
3.3
|
25.3
|
1.0
|
HZ
|
C:PHE308
|
3.7
|
28.8
|
1.0
|
HD2
|
C:HIS110
|
3.7
|
30.3
|
1.0
|
HD12
|
C:ILE109
|
3.7
|
28.2
|
1.0
|
HD11
|
C:ILE109
|
3.7
|
28.2
|
1.0
|
HG13
|
C:ILE109
|
3.8
|
27.4
|
1.0
|
HE2
|
C:PHE308
|
3.8
|
29.2
|
1.0
|
ND1
|
C:HIS119
|
4.0
|
22.7
|
1.0
|
HZ3
|
C:TRP118
|
4.0
|
26.8
|
1.0
|
ND1
|
C:HIS110
|
4.0
|
26.5
|
1.0
|
ND1
|
C:HIS102
|
4.1
|
22.2
|
1.0
|
CG
|
C:HIS102
|
4.1
|
22.5
|
1.0
|
CD1
|
C:ILE109
|
4.1
|
23.5
|
1.0
|
CG
|
C:HIS119
|
4.1
|
22.6
|
1.0
|
O
|
C:HOH2117
|
4.2
|
28.1
|
1.0
|
CG
|
C:HIS110
|
4.3
|
24.8
|
1.0
|
HE1
|
C:PHE115
|
4.3
|
27.4
|
1.0
|
CZ
|
C:PHE308
|
4.4
|
23.9
|
1.0
|
CU
|
C:CU2002
|
4.4
|
31.7
|
1.0
|
CE2
|
C:PHE308
|
4.5
|
24.3
|
1.0
|
CG1
|
C:ILE109
|
4.5
|
22.8
|
1.0
|
NE2
|
C:HIS312
|
4.6
|
25.6
|
1.0
|
CZ3
|
C:TRP118
|
4.6
|
22.4
|
1.0
|
HE1
|
C:HIS312
|
4.7
|
29.4
|
1.0
|
HD1
|
C:HIS110
|
4.8
|
31.8
|
1.0
|
HD1
|
C:HIS119
|
4.8
|
27.3
|
1.0
|
HD1
|
C:HIS102
|
4.8
|
26.6
|
1.0
|
HE3
|
C:TRP118
|
4.8
|
26.6
|
1.0
|
CE1
|
C:HIS312
|
4.9
|
24.5
|
1.0
|
HD1
|
C:PHE115
|
4.9
|
24.8
|
1.0
|
HG
|
C:SER302
|
5.0
|
32.2
|
1.0
|
|
Copper binding site 6 out
of 8 in 5or3
Go back to
Copper Binding Sites List in 5or3
Copper binding site 6 out
of 8 in the Crystal Structure of Aspergillus Oryzae Catechol Oxidase in Met/Deoxy- Form
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 6 of Crystal Structure of Aspergillus Oryzae Catechol Oxidase in Met/Deoxy- Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cu2002
b:31.7
occ:1.00
|
NE2
|
C:HIS288
|
1.9
|
27.2
|
1.0
|
O1
|
C:PER2009
|
2.0
|
37.9
|
1.0
|
NE2
|
C:HIS312
|
2.0
|
25.6
|
1.0
|
NE2
|
C:HIS284
|
2.1
|
26.7
|
1.0
|
O2
|
C:PER2009
|
2.6
|
30.1
|
1.0
|
CE1
|
C:HIS312
|
2.8
|
24.5
|
1.0
|
CD2
|
C:HIS288
|
2.9
|
28.9
|
1.0
|
HE1
|
C:HIS312
|
2.9
|
29.4
|
1.0
|
CE1
|
C:HIS288
|
3.0
|
27.4
|
1.0
|
CE1
|
C:HIS284
|
3.0
|
31.1
|
1.0
|
CD2
|
C:HIS284
|
3.0
|
26.6
|
1.0
|
HD2
|
C:HIS288
|
3.0
|
34.7
|
1.0
|
CD2
|
C:HIS312
|
3.1
|
24.9
|
1.0
|
HE1
|
C:HIS284
|
3.2
|
37.3
|
1.0
|
HE1
|
C:HIS288
|
3.2
|
32.9
|
1.0
|
HD2
|
C:HIS284
|
3.2
|
32.0
|
1.0
|
HD2
|
C:HIS312
|
3.4
|
29.9
|
1.0
|
HD2
|
C:HIS311
|
3.5
|
31.6
|
1.0
|
HE2
|
C:PHE308
|
3.5
|
29.2
|
1.0
|
ND1
|
C:HIS312
|
3.9
|
23.9
|
1.0
|
HE2
|
C:HIS311
|
4.0
|
30.3
|
1.0
|
ND1
|
C:HIS284
|
4.0
|
25.4
|
1.0
|
CG
|
C:HIS288
|
4.0
|
27.3
|
1.0
|
ND1
|
C:HIS288
|
4.0
|
28.3
|
1.0
|
CG
|
C:HIS284
|
4.1
|
24.3
|
1.0
|
CE2
|
C:PHE308
|
4.1
|
24.3
|
1.0
|
O
|
C:HOH2117
|
4.1
|
28.1
|
1.0
|
CG
|
C:HIS312
|
4.1
|
23.9
|
1.0
|
CD2
|
C:HIS311
|
4.2
|
26.3
|
1.0
|
HE1
|
C:PHE115
|
4.3
|
27.4
|
1.0
|
NE2
|
C:HIS311
|
4.4
|
25.2
|
1.0
|
CU
|
C:CU2001
|
4.4
|
27.2
|
1.0
|
HD2
|
C:HIS119
|
4.5
|
29.8
|
1.0
|
HZ
|
C:PHE308
|
4.6
|
28.8
|
1.0
|
NE2
|
C:HIS119
|
4.6
|
24.3
|
1.0
|
CZ
|
C:PHE308
|
4.7
|
23.9
|
1.0
|
HD1
|
C:HIS312
|
4.7
|
28.7
|
1.0
|
HD2
|
C:PHE308
|
4.7
|
30.8
|
1.0
|
CD2
|
C:PHE308
|
4.7
|
25.6
|
1.0
|
CD2
|
C:HIS119
|
4.7
|
24.8
|
1.0
|
HG13
|
C:ILE315
|
4.8
|
25.5
|
1.0
|
HD1
|
C:HIS284
|
4.8
|
30.5
|
1.0
|
HZ
|
C:PHE115
|
4.8
|
27.1
|
1.0
|
HD1
|
C:HIS288
|
4.8
|
33.9
|
1.0
|
HG
|
C:SER302
|
4.9
|
32.2
|
1.0
|
HD2
|
C:HIS110
|
4.9
|
30.3
|
1.0
|
OG
|
C:SER302
|
4.9
|
26.9
|
1.0
|
|
Copper binding site 7 out
of 8 in 5or3
Go back to
Copper Binding Sites List in 5or3
Copper binding site 7 out
of 8 in the Crystal Structure of Aspergillus Oryzae Catechol Oxidase in Met/Deoxy- Form
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 7 of Crystal Structure of Aspergillus Oryzae Catechol Oxidase in Met/Deoxy- Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cu2001
b:30.9
occ:1.00
|
NE2
|
D:HIS102
|
1.9
|
28.2
|
1.0
|
NE2
|
D:HIS119
|
2.0
|
28.6
|
1.0
|
O
|
D:HOH2140
|
2.1
|
29.6
|
1.0
|
NE2
|
D:HIS110
|
2.2
|
28.2
|
1.0
|
CE1
|
D:HIS102
|
2.9
|
27.1
|
1.0
|
CE1
|
D:HIS119
|
2.9
|
30.6
|
1.0
|
CE1
|
D:HIS110
|
3.0
|
31.1
|
1.0
|
CD2
|
D:HIS102
|
3.0
|
29.1
|
1.0
|
HE1
|
D:HIS110
|
3.0
|
37.4
|
1.0
|
HE1
|
D:HIS119
|
3.1
|
36.7
|
1.0
|
HE1
|
D:HIS102
|
3.1
|
32.6
|
1.0
|
CD2
|
D:HIS119
|
3.1
|
30.9
|
1.0
|
HD2
|
D:HIS102
|
3.2
|
34.9
|
1.0
|
CD2
|
D:HIS110
|
3.2
|
29.2
|
1.0
|
HD2
|
D:HIS119
|
3.4
|
37.1
|
1.0
|
HD2
|
D:HIS110
|
3.5
|
35.1
|
1.0
|
HD12
|
D:ILE109
|
3.6
|
33.6
|
1.0
|
HZ
|
D:PHE308
|
3.7
|
34.2
|
1.0
|
HD11
|
D:ILE109
|
3.9
|
33.6
|
1.0
|
HE2
|
D:PHE308
|
3.9
|
35.7
|
1.0
|
HG13
|
D:ILE109
|
3.9
|
33.4
|
1.0
|
HZ3
|
D:TRP118
|
4.0
|
34.1
|
1.0
|
ND1
|
D:HIS102
|
4.0
|
25.5
|
1.0
|
CG
|
D:HIS102
|
4.1
|
27.2
|
1.0
|
ND1
|
D:HIS119
|
4.1
|
27.5
|
1.0
|
ND1
|
D:HIS110
|
4.1
|
28.2
|
1.0
|
CD1
|
D:ILE109
|
4.1
|
28.0
|
1.0
|
CG
|
D:HIS119
|
4.2
|
29.6
|
1.0
|
O
|
D:HOH2178
|
4.3
|
29.4
|
1.0
|
CG
|
D:HIS110
|
4.3
|
27.8
|
1.0
|
HE1
|
D:PHE115
|
4.3
|
32.1
|
1.0
|
CU
|
D:CU2002
|
4.4
|
35.4
|
1.0
|
CZ
|
D:PHE308
|
4.5
|
28.5
|
1.0
|
CE2
|
D:PHE308
|
4.5
|
29.7
|
1.0
|
CZ3
|
D:TRP118
|
4.6
|
28.4
|
1.0
|
CG1
|
D:ILE109
|
4.6
|
27.8
|
1.0
|
HG
|
D:SER302
|
4.6
|
32.7
|
1.0
|
HE1
|
D:HIS312
|
4.6
|
37.6
|
1.0
|
NE2
|
D:HIS312
|
4.6
|
32.0
|
1.0
|
HE3
|
D:TRP118
|
4.7
|
32.6
|
1.0
|
HD1
|
D:HIS102
|
4.8
|
30.6
|
1.0
|
HD1
|
D:HIS110
|
4.8
|
33.9
|
1.0
|
CE1
|
D:HIS312
|
4.8
|
31.3
|
1.0
|
HD1
|
D:HIS119
|
4.8
|
33.0
|
1.0
|
HD1
|
D:PHE115
|
4.9
|
30.7
|
1.0
|
OG
|
D:SER302
|
4.9
|
27.3
|
1.0
|
CE3
|
D:TRP118
|
5.0
|
27.2
|
1.0
|
|
Copper binding site 8 out
of 8 in 5or3
Go back to
Copper Binding Sites List in 5or3
Copper binding site 8 out
of 8 in the Crystal Structure of Aspergillus Oryzae Catechol Oxidase in Met/Deoxy- Form
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 8 of Crystal Structure of Aspergillus Oryzae Catechol Oxidase in Met/Deoxy- Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cu2002
b:35.4
occ:1.00
|
NE2
|
D:HIS312
|
2.0
|
32.0
|
1.0
|
NE2
|
D:HIS288
|
2.0
|
30.3
|
1.0
|
NE2
|
D:HIS284
|
2.1
|
27.9
|
1.0
|
O
|
D:HOH2140
|
2.7
|
29.6
|
1.0
|
CE1
|
D:HIS312
|
2.8
|
31.3
|
1.0
|
HE1
|
D:HIS312
|
2.9
|
37.6
|
1.0
|
CD2
|
D:HIS288
|
2.9
|
30.0
|
1.0
|
CD2
|
D:HIS284
|
3.0
|
28.2
|
1.0
|
CE1
|
D:HIS288
|
3.0
|
30.6
|
1.0
|
CE1
|
D:HIS284
|
3.0
|
27.6
|
1.0
|
HD2
|
D:HIS288
|
3.1
|
36.0
|
1.0
|
CD2
|
D:HIS312
|
3.1
|
32.5
|
1.0
|
HD2
|
D:HIS284
|
3.1
|
33.9
|
1.0
|
HE1
|
D:HIS288
|
3.2
|
36.7
|
1.0
|
HE1
|
D:HIS284
|
3.3
|
33.1
|
1.0
|
HD2
|
D:HIS312
|
3.4
|
39.0
|
1.0
|
HD2
|
D:HIS311
|
3.4
|
35.7
|
1.0
|
HE2
|
D:PHE308
|
3.5
|
35.7
|
1.0
|
HE2
|
D:HIS311
|
3.9
|
35.5
|
1.0
|
ND1
|
D:HIS312
|
3.9
|
34.1
|
1.0
|
CE2
|
D:PHE308
|
4.0
|
29.7
|
1.0
|
CG
|
D:HIS284
|
4.0
|
28.1
|
1.0
|
ND1
|
D:HIS284
|
4.0
|
27.6
|
1.0
|
CG
|
D:HIS288
|
4.1
|
28.9
|
1.0
|
O
|
D:HOH2178
|
4.1
|
29.4
|
1.0
|
ND1
|
D:HIS288
|
4.1
|
29.4
|
1.0
|
CG
|
D:HIS312
|
4.1
|
31.2
|
1.0
|
CD2
|
D:HIS311
|
4.1
|
29.8
|
1.0
|
HG
|
D:SER302
|
4.2
|
32.7
|
1.0
|
HE1
|
D:PHE115
|
4.2
|
32.1
|
1.0
|
NE2
|
D:HIS311
|
4.3
|
29.6
|
1.0
|
HD2
|
D:HIS119
|
4.4
|
37.1
|
1.0
|
CU
|
D:CU2001
|
4.4
|
30.9
|
1.0
|
NE2
|
D:HIS119
|
4.5
|
28.6
|
1.0
|
HZ
|
D:PHE308
|
4.6
|
34.2
|
1.0
|
CD2
|
D:HIS119
|
4.6
|
30.9
|
1.0
|
HD1
|
D:HIS312
|
4.7
|
40.9
|
1.0
|
CZ
|
D:PHE308
|
4.7
|
28.5
|
1.0
|
HG13
|
D:ILE315
|
4.7
|
31.7
|
1.0
|
HZ
|
D:PHE115
|
4.7
|
33.5
|
1.0
|
HD2
|
D:PHE308
|
4.7
|
35.1
|
1.0
|
CD2
|
D:PHE308
|
4.7
|
29.2
|
1.0
|
HD1
|
D:HIS284
|
4.8
|
33.1
|
1.0
|
HD2
|
D:HIS110
|
4.8
|
35.1
|
1.0
|
HD1
|
D:HIS288
|
4.9
|
35.2
|
1.0
|
OG
|
D:SER302
|
4.9
|
27.3
|
1.0
|
|
Reference:
L.Penttinen,
C.Rutanen,
M.Saloheimo,
K.Kruus,
J.Rouvinen,
N.Hakulinen.
A New Crystal Form of Aspergillus Oryzae Catechol Oxidase and Evaluation of Copper Site Structures in Coupled Binuclear Copper Enzymes. Plos One V. 13 96691 2018.
ISSN: ESSN 1932-6203
PubMed: 29715329
DOI: 10.1371/JOURNAL.PONE.0196691
Page generated: Wed Jul 31 05:09:05 2024
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