Copper in PDB 9f3z: Psychrophilic Laccase (Multicopper Oxidase) From Oenococcus Oeni 229 with Histag
Protein crystallography data
The structure of Psychrophilic Laccase (Multicopper Oxidase) From Oenococcus Oeni 229 with Histag, PDB code: 9f3z
was solved by
F.Paredes,
P.Casino,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
93.61 /
3.50
|
Space group
|
I 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
106.05,
56.69,
182.296,
90,
92.87,
90
|
R / Rfree (%)
|
20.8 /
25.7
|
Copper Binding Sites:
The binding sites of Copper atom in the Psychrophilic Laccase (Multicopper Oxidase) From Oenococcus Oeni 229 with Histag
(pdb code 9f3z). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 8 binding sites of Copper where determined in the
Psychrophilic Laccase (Multicopper Oxidase) From Oenococcus Oeni 229 with Histag, PDB code: 9f3z:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Copper binding site 1 out
of 8 in 9f3z
Go back to
Copper Binding Sites List in 9f3z
Copper binding site 1 out
of 8 in the Psychrophilic Laccase (Multicopper Oxidase) From Oenococcus Oeni 229 with Histag
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Psychrophilic Laccase (Multicopper Oxidase) From Oenococcus Oeni 229 with Histag within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu501
b:177.8
occ:1.00
|
SG
|
B:CYS446
|
2.0
|
66.4
|
1.0
|
ND1
|
B:HIS451
|
2.1
|
67.2
|
1.0
|
ND1
|
B:HIS392
|
2.4
|
62.1
|
1.0
|
CB
|
B:CYS446
|
2.9
|
59.9
|
1.0
|
SD
|
B:MET456
|
3.0
|
59.8
|
1.0
|
CG
|
B:HIS451
|
3.1
|
67.8
|
1.0
|
CE1
|
B:HIS392
|
3.1
|
63.6
|
1.0
|
CE1
|
B:HIS451
|
3.1
|
68.0
|
1.0
|
CB
|
B:HIS451
|
3.3
|
68.4
|
1.0
|
CG
|
B:HIS392
|
3.6
|
61.8
|
1.0
|
CB
|
B:HIS392
|
4.1
|
59.5
|
1.0
|
CE
|
B:MET456
|
4.1
|
60.8
|
1.0
|
NE2
|
B:HIS451
|
4.2
|
66.8
|
1.0
|
CD2
|
B:HIS451
|
4.2
|
66.8
|
1.0
|
CD1
|
B:ILE448
|
4.2
|
54.0
|
1.0
|
CG1
|
B:VAL352
|
4.2
|
80.0
|
1.0
|
NE2
|
B:HIS392
|
4.3
|
62.8
|
1.0
|
CA
|
B:CYS446
|
4.3
|
57.6
|
1.0
|
CG
|
B:MET456
|
4.5
|
57.0
|
1.0
|
CE
|
B:MET345
|
4.5
|
78.3
|
1.0
|
CD2
|
B:HIS392
|
4.5
|
63.1
|
1.0
|
CB
|
B:ILE448
|
4.6
|
51.4
|
1.0
|
CA
|
B:HIS392
|
4.7
|
57.1
|
1.0
|
CG1
|
B:ILE448
|
4.8
|
53.2
|
1.0
|
CB
|
B:MET456
|
4.8
|
54.6
|
1.0
|
CA
|
B:HIS451
|
4.8
|
67.8
|
1.0
|
C
|
B:CYS446
|
4.9
|
59.8
|
1.0
|
|
Copper binding site 2 out
of 8 in 9f3z
Go back to
Copper Binding Sites List in 9f3z
Copper binding site 2 out
of 8 in the Psychrophilic Laccase (Multicopper Oxidase) From Oenococcus Oeni 229 with Histag
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Psychrophilic Laccase (Multicopper Oxidase) From Oenococcus Oeni 229 with Histag within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu502
b:90.7
occ:1.00
|
NE2
|
B:HIS395
|
1.8
|
52.3
|
1.0
|
NE2
|
B:HIS106
|
2.0
|
58.4
|
1.0
|
CD2
|
B:HIS395
|
2.8
|
50.9
|
1.0
|
CE1
|
B:HIS106
|
2.8
|
58.6
|
1.0
|
CE1
|
B:HIS395
|
2.9
|
53.4
|
1.0
|
CD2
|
B:HIS106
|
3.0
|
55.7
|
1.0
|
CG
|
B:HIS108
|
3.1
|
42.5
|
1.0
|
ND1
|
B:HIS108
|
3.2
|
42.9
|
1.0
|
CB
|
B:HIS108
|
3.3
|
42.7
|
1.0
|
CA
|
B:HIS108
|
3.4
|
42.4
|
1.0
|
CD2
|
B:HIS397
|
3.5
|
52.3
|
1.0
|
CU
|
B:CU503
|
3.6
|
53.5
|
1.0
|
NE2
|
B:HIS397
|
3.7
|
54.7
|
1.0
|
CD2
|
B:HIS108
|
3.7
|
42.7
|
1.0
|
CE1
|
B:HIS108
|
3.8
|
43.6
|
1.0
|
CU
|
B:CU504
|
3.8
|
71.8
|
1.0
|
ND1
|
B:HIS106
|
3.9
|
54.9
|
1.0
|
CG
|
B:HIS395
|
3.9
|
49.2
|
1.0
|
ND1
|
B:HIS395
|
3.9
|
52.0
|
1.0
|
CG
|
B:HIS106
|
4.0
|
53.9
|
1.0
|
NE2
|
B:HIS108
|
4.1
|
43.2
|
1.0
|
CG
|
B:HIS397
|
4.2
|
51.4
|
1.0
|
N
|
B:HIS108
|
4.3
|
42.3
|
1.0
|
C
|
B:HIS108
|
4.4
|
41.9
|
1.0
|
N
|
B:GLY109
|
4.6
|
44.9
|
1.0
|
CE1
|
B:HIS397
|
4.6
|
55.8
|
1.0
|
NE2
|
B:HIS147
|
4.6
|
40.5
|
1.0
|
O
|
B:TRP107
|
4.8
|
38.3
|
1.0
|
CA
|
B:HIS397
|
4.8
|
52.1
|
1.0
|
C
|
B:TRP107
|
4.8
|
42.7
|
1.0
|
ND1
|
B:HIS397
|
4.8
|
53.8
|
1.0
|
CB
|
B:HIS397
|
5.0
|
51.2
|
1.0
|
NE2
|
B:HIS445
|
5.0
|
69.7
|
1.0
|
|
Copper binding site 3 out
of 8 in 9f3z
Go back to
Copper Binding Sites List in 9f3z
Copper binding site 3 out
of 8 in the Psychrophilic Laccase (Multicopper Oxidase) From Oenococcus Oeni 229 with Histag
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Psychrophilic Laccase (Multicopper Oxidase) From Oenococcus Oeni 229 with Histag within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu503
b:53.5
occ:1.00
|
NE2
|
B:HIS147
|
1.8
|
40.5
|
1.0
|
ND1
|
B:HIS108
|
2.0
|
42.9
|
1.0
|
NE2
|
B:HIS447
|
2.1
|
44.4
|
1.0
|
CE1
|
B:HIS147
|
2.6
|
41.1
|
1.0
|
CE1
|
B:HIS108
|
2.8
|
43.6
|
1.0
|
CD2
|
B:HIS447
|
2.9
|
45.0
|
1.0
|
CD2
|
B:HIS147
|
3.0
|
38.8
|
1.0
|
CG
|
B:HIS108
|
3.2
|
42.5
|
1.0
|
CE1
|
B:HIS447
|
3.2
|
45.4
|
1.0
|
CU
|
B:CU502
|
3.6
|
90.7
|
1.0
|
CB
|
B:HIS108
|
3.6
|
42.7
|
1.0
|
CD2
|
B:HIS395
|
3.7
|
50.9
|
1.0
|
ND1
|
B:HIS147
|
3.8
|
40.5
|
1.0
|
CD2
|
B:HIS106
|
3.9
|
55.7
|
1.0
|
CU
|
B:CU504
|
3.9
|
71.8
|
1.0
|
NE2
|
B:HIS395
|
3.9
|
52.3
|
1.0
|
CG
|
B:HIS147
|
4.0
|
38.3
|
1.0
|
NE2
|
B:HIS108
|
4.0
|
43.2
|
1.0
|
CG
|
B:HIS447
|
4.1
|
46.6
|
1.0
|
NE2
|
B:HIS106
|
4.1
|
58.4
|
1.0
|
CD2
|
B:HIS108
|
4.2
|
42.7
|
1.0
|
CZ2
|
B:TRP145
|
4.2
|
45.5
|
1.0
|
ND1
|
B:HIS447
|
4.2
|
45.0
|
1.0
|
CE2
|
B:TRP145
|
4.6
|
44.4
|
1.0
|
NE1
|
B:TRP145
|
4.6
|
44.3
|
1.0
|
CG
|
B:HIS395
|
4.7
|
49.2
|
1.0
|
CE1
|
B:HIS445
|
4.8
|
67.0
|
1.0
|
CB
|
B:ALA281
|
4.8
|
44.4
|
1.0
|
CA
|
B:HIS108
|
4.9
|
42.4
|
1.0
|
CE1
|
B:HIS395
|
5.0
|
53.4
|
1.0
|
NE2
|
B:HIS445
|
5.0
|
69.7
|
1.0
|
CH2
|
B:TRP145
|
5.0
|
45.8
|
1.0
|
|
Copper binding site 4 out
of 8 in 9f3z
Go back to
Copper Binding Sites List in 9f3z
Copper binding site 4 out
of 8 in the Psychrophilic Laccase (Multicopper Oxidase) From Oenococcus Oeni 229 with Histag
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of Psychrophilic Laccase (Multicopper Oxidase) From Oenococcus Oeni 229 with Histag within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu504
b:71.8
occ:1.00
|
NE2
|
B:HIS149
|
2.0
|
81.4
|
1.0
|
NE2
|
B:HIS445
|
2.0
|
69.7
|
1.0
|
NE2
|
B:HIS397
|
2.2
|
54.7
|
1.0
|
CD2
|
B:HIS149
|
2.4
|
78.4
|
1.0
|
CE1
|
B:HIS445
|
2.4
|
67.0
|
1.0
|
CE1
|
B:HIS397
|
3.1
|
55.8
|
1.0
|
CE1
|
B:HIS149
|
3.3
|
81.2
|
1.0
|
CD2
|
B:HIS106
|
3.3
|
55.7
|
1.0
|
CD2
|
B:HIS445
|
3.3
|
68.6
|
1.0
|
CD2
|
B:HIS397
|
3.3
|
52.3
|
1.0
|
NE2
|
B:HIS106
|
3.3
|
58.4
|
1.0
|
CG
|
B:HIS149
|
3.6
|
70.6
|
1.0
|
ND1
|
B:HIS445
|
3.7
|
65.2
|
1.0
|
CD2
|
B:HIS395
|
3.7
|
50.9
|
1.0
|
CU
|
B:CU502
|
3.8
|
90.7
|
1.0
|
CU
|
B:CU503
|
3.9
|
53.5
|
1.0
|
ND1
|
B:HIS149
|
4.0
|
76.2
|
1.0
|
CG
|
B:HIS445
|
4.1
|
64.5
|
1.0
|
ND1
|
B:HIS397
|
4.2
|
53.8
|
1.0
|
NE2
|
B:HIS395
|
4.2
|
52.3
|
1.0
|
CE1
|
B:HIS147
|
4.3
|
41.1
|
1.0
|
CG
|
B:HIS397
|
4.4
|
51.4
|
1.0
|
CG
|
B:HIS106
|
4.4
|
53.9
|
1.0
|
CE1
|
B:HIS106
|
4.4
|
58.6
|
1.0
|
CD2
|
B:HIS447
|
4.7
|
45.0
|
1.0
|
NE2
|
B:HIS147
|
4.7
|
40.5
|
1.0
|
NE2
|
B:HIS447
|
4.8
|
44.4
|
1.0
|
CB
|
B:HIS149
|
4.9
|
58.2
|
1.0
|
CG
|
B:HIS395
|
4.9
|
49.2
|
1.0
|
ND1
|
B:HIS106
|
5.0
|
54.9
|
1.0
|
|
Copper binding site 5 out
of 8 in 9f3z
Go back to
Copper Binding Sites List in 9f3z
Copper binding site 5 out
of 8 in the Psychrophilic Laccase (Multicopper Oxidase) From Oenococcus Oeni 229 with Histag
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 5 of Psychrophilic Laccase (Multicopper Oxidase) From Oenococcus Oeni 229 with Histag within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu501
b:113.8
occ:1.00
|
ND1
|
A:HIS451
|
2.0
|
62.9
|
1.0
|
SG
|
A:CYS446
|
2.2
|
86.9
|
1.0
|
ND1
|
A:HIS392
|
2.3
|
71.1
|
1.0
|
CE1
|
A:HIS392
|
2.8
|
76.5
|
1.0
|
CB
|
A:CYS446
|
2.8
|
73.1
|
1.0
|
CE1
|
A:HIS451
|
2.9
|
60.6
|
1.0
|
CG
|
A:HIS451
|
3.0
|
63.1
|
1.0
|
CB
|
A:HIS451
|
3.3
|
64.2
|
1.0
|
SD
|
A:MET456
|
3.4
|
74.5
|
1.0
|
CG
|
A:HIS392
|
3.6
|
66.5
|
1.0
|
NE2
|
A:HIS451
|
4.0
|
61.7
|
1.0
|
NE2
|
A:HIS392
|
4.1
|
76.1
|
1.0
|
CD2
|
A:HIS451
|
4.1
|
63.1
|
1.0
|
CG1
|
A:VAL352
|
4.2
|
74.3
|
1.0
|
CB
|
A:HIS392
|
4.2
|
61.4
|
1.0
|
CA
|
A:CYS446
|
4.3
|
67.6
|
1.0
|
CD1
|
A:ILE448
|
4.3
|
69.2
|
1.0
|
CE
|
A:MET456
|
4.4
|
74.5
|
1.0
|
CD2
|
A:HIS392
|
4.4
|
69.0
|
1.0
|
CG
|
A:MET456
|
4.5
|
75.2
|
1.0
|
CB
|
A:ILE448
|
4.5
|
65.0
|
1.0
|
CB
|
A:MET456
|
4.7
|
74.7
|
1.0
|
CE
|
A:MET345
|
4.8
|
89.4
|
1.0
|
CG1
|
A:ILE448
|
4.8
|
68.3
|
1.0
|
CA
|
A:HIS392
|
4.8
|
59.0
|
1.0
|
CA
|
A:HIS451
|
4.8
|
66.6
|
1.0
|
C
|
A:CYS446
|
4.8
|
61.6
|
1.0
|
O
|
A:ILE448
|
4.9
|
67.9
|
1.0
|
|
Copper binding site 6 out
of 8 in 9f3z
Go back to
Copper Binding Sites List in 9f3z
Copper binding site 6 out
of 8 in the Psychrophilic Laccase (Multicopper Oxidase) From Oenococcus Oeni 229 with Histag
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 6 of Psychrophilic Laccase (Multicopper Oxidase) From Oenococcus Oeni 229 with Histag within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu502
b:109.9
occ:1.00
|
NE2
|
A:HIS106
|
1.9
|
85.1
|
1.0
|
NE2
|
A:HIS395
|
1.9
|
76.4
|
1.0
|
CE1
|
A:HIS106
|
2.6
|
87.0
|
1.0
|
CD2
|
A:HIS395
|
2.8
|
73.6
|
1.0
|
CD2
|
A:HIS397
|
2.9
|
79.5
|
1.0
|
CE1
|
A:HIS395
|
3.0
|
76.2
|
1.0
|
CD2
|
A:HIS106
|
3.0
|
83.8
|
1.0
|
NE2
|
A:HIS397
|
3.2
|
81.4
|
1.0
|
CG
|
A:HIS397
|
3.7
|
78.2
|
1.0
|
CG
|
A:HIS108
|
3.7
|
73.3
|
1.0
|
CU
|
A:CU504
|
3.7
|
78.6
|
1.0
|
ND1
|
A:HIS108
|
3.7
|
73.6
|
1.0
|
ND1
|
A:HIS106
|
3.8
|
85.2
|
1.0
|
CA
|
A:HIS108
|
3.8
|
72.0
|
1.0
|
CU
|
A:CU503
|
3.9
|
58.2
|
1.0
|
CB
|
A:HIS108
|
3.9
|
71.4
|
1.0
|
CG
|
A:HIS395
|
4.0
|
71.2
|
1.0
|
CG
|
A:HIS106
|
4.0
|
81.9
|
1.0
|
ND1
|
A:HIS395
|
4.0
|
74.6
|
1.0
|
CE1
|
A:HIS397
|
4.1
|
81.6
|
1.0
|
CD2
|
A:HIS108
|
4.3
|
75.7
|
1.0
|
CE1
|
A:HIS108
|
4.3
|
73.7
|
1.0
|
ND1
|
A:HIS397
|
4.3
|
79.4
|
1.0
|
CA
|
A:HIS397
|
4.3
|
79.1
|
1.0
|
CB
|
A:HIS397
|
4.5
|
78.0
|
1.0
|
NE2
|
A:HIS108
|
4.6
|
74.1
|
1.0
|
NE2
|
A:HIS445
|
4.6
|
73.1
|
1.0
|
N
|
A:HIS397
|
4.6
|
74.3
|
1.0
|
N
|
A:HIS108
|
4.7
|
73.1
|
1.0
|
C
|
A:HIS108
|
4.8
|
71.3
|
1.0
|
N
|
A:GLY109
|
4.9
|
73.3
|
1.0
|
O
|
A:MET396
|
4.9
|
67.7
|
1.0
|
C
|
A:MET396
|
4.9
|
72.9
|
1.0
|
O
|
A:TRP107
|
4.9
|
72.7
|
1.0
|
NE2
|
A:HIS147
|
5.0
|
63.8
|
1.0
|
|
Copper binding site 7 out
of 8 in 9f3z
Go back to
Copper Binding Sites List in 9f3z
Copper binding site 7 out
of 8 in the Psychrophilic Laccase (Multicopper Oxidase) From Oenococcus Oeni 229 with Histag
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 7 of Psychrophilic Laccase (Multicopper Oxidase) From Oenococcus Oeni 229 with Histag within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu503
b:58.2
occ:1.00
|
NE2
|
A:HIS147
|
1.9
|
63.8
|
1.0
|
ND1
|
A:HIS108
|
2.0
|
73.6
|
1.0
|
NE2
|
A:HIS447
|
2.2
|
64.6
|
1.0
|
CE1
|
A:HIS108
|
2.8
|
73.7
|
1.0
|
CE1
|
A:HIS147
|
2.8
|
65.0
|
1.0
|
CD2
|
A:HIS447
|
3.0
|
64.9
|
1.0
|
CD2
|
A:HIS147
|
3.0
|
63.0
|
1.0
|
CG
|
A:HIS108
|
3.1
|
73.3
|
1.0
|
CE1
|
A:HIS447
|
3.3
|
65.4
|
1.0
|
CB
|
A:HIS108
|
3.6
|
71.4
|
1.0
|
CD2
|
A:HIS395
|
3.7
|
73.6
|
1.0
|
CU
|
A:CU502
|
3.9
|
109.9
|
1.0
|
CD2
|
A:HIS106
|
3.9
|
83.8
|
1.0
|
NE2
|
A:HIS395
|
3.9
|
76.4
|
1.0
|
ND1
|
A:HIS147
|
3.9
|
64.1
|
1.0
|
NE2
|
A:HIS108
|
3.9
|
74.1
|
1.0
|
CU
|
A:CU504
|
4.0
|
78.6
|
1.0
|
CG
|
A:HIS147
|
4.1
|
63.0
|
1.0
|
CD2
|
A:HIS108
|
4.1
|
75.7
|
1.0
|
NE2
|
A:HIS106
|
4.1
|
85.1
|
1.0
|
CG
|
A:HIS447
|
4.1
|
65.2
|
1.0
|
CZ2
|
A:TRP145
|
4.2
|
57.7
|
1.0
|
ND1
|
A:HIS447
|
4.2
|
66.7
|
1.0
|
NE1
|
A:TRP145
|
4.5
|
60.2
|
1.0
|
CE2
|
A:TRP145
|
4.5
|
58.8
|
1.0
|
CG
|
A:HIS395
|
4.7
|
71.2
|
1.0
|
CA
|
A:HIS108
|
4.8
|
72.0
|
1.0
|
CB
|
A:ALA281
|
4.8
|
74.0
|
1.0
|
CE1
|
A:HIS445
|
4.9
|
71.1
|
1.0
|
CE1
|
A:HIS395
|
4.9
|
76.2
|
1.0
|
NE2
|
A:HIS445
|
5.0
|
73.1
|
1.0
|
|
Copper binding site 8 out
of 8 in 9f3z
Go back to
Copper Binding Sites List in 9f3z
Copper binding site 8 out
of 8 in the Psychrophilic Laccase (Multicopper Oxidase) From Oenococcus Oeni 229 with Histag
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 8 of Psychrophilic Laccase (Multicopper Oxidase) From Oenococcus Oeni 229 with Histag within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu504
b:78.6
occ:1.00
|
NE2
|
A:HIS445
|
2.0
|
73.1
|
1.0
|
CE1
|
A:HIS445
|
2.2
|
71.1
|
1.0
|
NE2
|
A:HIS149
|
2.2
|
91.4
|
1.0
|
NE2
|
A:HIS397
|
2.3
|
81.4
|
1.0
|
CD2
|
A:HIS149
|
2.5
|
85.8
|
1.0
|
CE1
|
A:HIS397
|
3.2
|
81.6
|
1.0
|
CD2
|
A:HIS445
|
3.3
|
70.9
|
1.0
|
ND1
|
A:HIS445
|
3.4
|
70.5
|
1.0
|
CD2
|
A:HIS397
|
3.4
|
79.5
|
1.0
|
CE1
|
A:HIS149
|
3.4
|
95.6
|
1.0
|
CD2
|
A:HIS106
|
3.5
|
83.8
|
1.0
|
NE2
|
A:HIS106
|
3.5
|
85.1
|
1.0
|
CU
|
A:CU502
|
3.7
|
109.9
|
1.0
|
CG
|
A:HIS149
|
3.7
|
83.5
|
1.0
|
CD2
|
A:HIS395
|
3.9
|
73.6
|
1.0
|
CG
|
A:HIS445
|
4.0
|
71.2
|
1.0
|
CU
|
A:CU503
|
4.0
|
58.2
|
1.0
|
ND1
|
A:HIS149
|
4.2
|
92.9
|
1.0
|
ND1
|
A:HIS397
|
4.4
|
79.4
|
1.0
|
NE2
|
A:HIS395
|
4.4
|
76.4
|
1.0
|
CE1
|
A:HIS147
|
4.4
|
65.0
|
1.0
|
CG
|
A:HIS397
|
4.5
|
78.2
|
1.0
|
CG
|
A:HIS106
|
4.6
|
81.9
|
1.0
|
CD2
|
A:HIS447
|
4.6
|
64.9
|
1.0
|
CE1
|
A:HIS106
|
4.6
|
87.0
|
1.0
|
NE2
|
A:HIS447
|
4.7
|
64.6
|
1.0
|
NE2
|
A:HIS147
|
4.8
|
63.8
|
1.0
|
CB
|
A:HIS149
|
4.9
|
77.8
|
1.0
|
CB
|
A:MET443
|
5.0
|
93.1
|
1.0
|
|
Reference:
I.Olmeda,
F.Paredes,
R.Sendra,
P.Casino,
I.Pardo,
S.Ferrer.
Biochemical and Structural Characterization of A Novel Psychrophilic Laccase (Multicopper Oxidase) Discovered From Oenococcus Oeni 229 (Enolab 4002). Int J Mol Sci 2024.
ISSN: ESSN 1422-0067
Page generated: Sun Aug 11 11:03:08 2024
|