Copper in PDB 6juc: Aspergillus Oryzae Pro-Tyrosinase Oxygen-Bound C92A/H103F Mutant
Enzymatic activity of Aspergillus Oryzae Pro-Tyrosinase Oxygen-Bound C92A/H103F Mutant
All present enzymatic activity of Aspergillus Oryzae Pro-Tyrosinase Oxygen-Bound C92A/H103F Mutant:
1.14.18.1;
Protein crystallography data
The structure of Aspergillus Oryzae Pro-Tyrosinase Oxygen-Bound C92A/H103F Mutant, PDB code: 6juc
was solved by
N.Fujieda,
K.Umakoshi,
Y.Nishikawa,
G.Kurisu,
S.Itoh,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
30.00 /
1.44
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
54.118,
118.027,
79.071,
90.00,
91.21,
90.00
|
R / Rfree (%)
|
17 /
22.5
|
Copper Binding Sites:
The binding sites of Copper atom in the Aspergillus Oryzae Pro-Tyrosinase Oxygen-Bound C92A/H103F Mutant
(pdb code 6juc). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the
Aspergillus Oryzae Pro-Tyrosinase Oxygen-Bound C92A/H103F Mutant, PDB code: 6juc:
Jump to Copper binding site number:
1;
2;
3;
4;
Copper binding site 1 out
of 4 in 6juc
Go back to
Copper Binding Sites List in 6juc
Copper binding site 1 out
of 4 in the Aspergillus Oryzae Pro-Tyrosinase Oxygen-Bound C92A/H103F Mutant
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Aspergillus Oryzae Pro-Tyrosinase Oxygen-Bound C92A/H103F Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu701
b:18.8
occ:0.51
|
O
|
A:HOH1034
|
1.5
|
27.6
|
1.0
|
NE2
|
A:HIS94
|
2.0
|
20.7
|
1.0
|
NE2
|
A:HIS67
|
2.0
|
15.9
|
1.0
|
CE1
|
A:HIS67
|
2.9
|
15.3
|
1.0
|
CD2
|
A:HIS94
|
3.0
|
20.2
|
1.0
|
CE1
|
A:HIS94
|
3.0
|
20.2
|
1.0
|
CD2
|
A:HIS67
|
3.1
|
14.5
|
1.0
|
CZ
|
A:PHE103
|
3.3
|
13.1
|
1.0
|
CE2
|
A:PHE513
|
3.6
|
17.0
|
1.0
|
CU
|
A:CU702
|
3.8
|
18.7
|
0.8
|
ND1
|
A:HIS67
|
4.0
|
15.6
|
1.0
|
CE1
|
A:PHE103
|
4.1
|
14.9
|
1.0
|
ND1
|
A:HIS94
|
4.1
|
19.4
|
1.0
|
CE2
|
A:PHE103
|
4.1
|
12.4
|
1.0
|
CG
|
A:HIS94
|
4.1
|
18.0
|
1.0
|
CG
|
A:HIS67
|
4.2
|
13.7
|
1.0
|
CZ
|
A:PHE513
|
4.2
|
16.1
|
1.0
|
CE2
|
A:PHE368
|
4.5
|
14.4
|
1.0
|
NE2
|
A:HIS328
|
4.5
|
15.4
|
1.0
|
NE2
|
A:HIS372
|
4.6
|
14.5
|
1.0
|
CD2
|
A:PHE513
|
4.6
|
16.9
|
1.0
|
CB
|
A:ALA92
|
4.6
|
17.5
|
1.0
|
CZ
|
A:PHE368
|
4.7
|
14.2
|
1.0
|
CE1
|
A:HIS328
|
4.7
|
15.1
|
1.0
|
NE2
|
A:HIS332
|
4.8
|
14.9
|
1.0
|
CG1
|
A:VAL359
|
4.9
|
23.2
|
1.0
|
|
Copper binding site 2 out
of 4 in 6juc
Go back to
Copper Binding Sites List in 6juc
Copper binding site 2 out
of 4 in the Aspergillus Oryzae Pro-Tyrosinase Oxygen-Bound C92A/H103F Mutant
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Aspergillus Oryzae Pro-Tyrosinase Oxygen-Bound C92A/H103F Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu702
b:18.7
occ:0.83
|
NE2
|
A:HIS332
|
2.0
|
14.9
|
1.0
|
NE2
|
A:HIS372
|
2.0
|
14.5
|
1.0
|
NE2
|
A:HIS328
|
2.2
|
15.4
|
1.0
|
O
|
A:HOH1034
|
2.3
|
27.6
|
1.0
|
CE1
|
A:HIS372
|
2.9
|
14.4
|
1.0
|
CD2
|
A:HIS372
|
2.9
|
13.5
|
1.0
|
CE1
|
A:HIS332
|
3.0
|
14.8
|
1.0
|
CD2
|
A:HIS328
|
3.0
|
16.1
|
1.0
|
CD2
|
A:HIS332
|
3.0
|
13.8
|
1.0
|
CE1
|
A:HIS328
|
3.2
|
15.1
|
1.0
|
CE2
|
A:PHE368
|
3.7
|
14.4
|
1.0
|
CU
|
A:CU701
|
3.8
|
18.8
|
0.5
|
ND1
|
A:HIS372
|
4.0
|
13.5
|
1.0
|
CG
|
A:HIS372
|
4.1
|
13.6
|
1.0
|
ND1
|
A:HIS332
|
4.1
|
12.3
|
1.0
|
CG
|
A:HIS332
|
4.1
|
13.7
|
1.0
|
CG
|
A:HIS328
|
4.2
|
14.6
|
1.0
|
CE2
|
A:PHE513
|
4.2
|
17.0
|
1.0
|
ND1
|
A:HIS328
|
4.2
|
15.1
|
1.0
|
CD2
|
A:PHE368
|
4.3
|
12.8
|
1.0
|
CD2
|
A:HIS371
|
4.3
|
13.1
|
1.0
|
CZ
|
A:PHE368
|
4.4
|
14.2
|
1.0
|
CZ
|
A:PHE513
|
4.5
|
16.1
|
1.0
|
NE2
|
A:HIS371
|
4.7
|
11.9
|
1.0
|
CE1
|
A:PHE103
|
4.7
|
14.9
|
1.0
|
CZ
|
A:PHE103
|
4.7
|
13.1
|
1.0
|
NE2
|
A:HIS67
|
4.9
|
15.9
|
1.0
|
|
Copper binding site 3 out
of 4 in 6juc
Go back to
Copper Binding Sites List in 6juc
Copper binding site 3 out
of 4 in the Aspergillus Oryzae Pro-Tyrosinase Oxygen-Bound C92A/H103F Mutant
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Aspergillus Oryzae Pro-Tyrosinase Oxygen-Bound C92A/H103F Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu701
b:16.1
occ:0.66
|
O1
|
B:PER703
|
1.6
|
20.5
|
0.8
|
O2
|
B:PER703
|
1.9
|
17.8
|
0.8
|
NE2
|
B:HIS94
|
1.9
|
18.0
|
1.0
|
NE2
|
B:HIS67
|
2.0
|
13.9
|
1.0
|
CE1
|
B:HIS67
|
2.8
|
14.9
|
1.0
|
CE1
|
B:HIS94
|
2.9
|
18.0
|
1.0
|
CD2
|
B:HIS94
|
3.0
|
18.6
|
1.0
|
CD2
|
B:HIS67
|
3.2
|
14.1
|
1.0
|
CZ
|
B:PHE103
|
3.2
|
15.4
|
1.0
|
CU
|
B:CU702
|
3.5
|
19.1
|
0.9
|
CE2
|
B:PHE513
|
3.6
|
15.8
|
1.0
|
CE2
|
B:PHE103
|
4.0
|
15.1
|
1.0
|
CE1
|
B:PHE103
|
4.0
|
15.2
|
1.0
|
ND1
|
B:HIS94
|
4.0
|
18.1
|
1.0
|
ND1
|
B:HIS67
|
4.0
|
14.4
|
1.0
|
CG
|
B:HIS94
|
4.1
|
19.0
|
1.0
|
CG
|
B:HIS67
|
4.2
|
13.8
|
1.0
|
CZ
|
B:PHE513
|
4.2
|
15.3
|
1.0
|
CB
|
B:ALA92
|
4.5
|
17.6
|
1.0
|
CE2
|
B:PHE368
|
4.5
|
15.1
|
1.0
|
NE2
|
B:HIS328
|
4.6
|
15.1
|
1.0
|
NE2
|
B:HIS372
|
4.6
|
15.5
|
1.0
|
CD2
|
B:PHE513
|
4.7
|
15.4
|
1.0
|
CE1
|
B:HIS328
|
4.7
|
16.5
|
1.0
|
CZ
|
B:PHE368
|
4.7
|
17.4
|
1.0
|
NE2
|
B:HIS332
|
4.8
|
15.2
|
1.0
|
|
Copper binding site 4 out
of 4 in 6juc
Go back to
Copper Binding Sites List in 6juc
Copper binding site 4 out
of 4 in the Aspergillus Oryzae Pro-Tyrosinase Oxygen-Bound C92A/H103F Mutant
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of Aspergillus Oryzae Pro-Tyrosinase Oxygen-Bound C92A/H103F Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu702
b:19.1
occ:0.87
|
O2
|
B:PER703
|
1.8
|
17.8
|
0.8
|
NE2
|
B:HIS328
|
2.0
|
15.1
|
1.0
|
NE2
|
B:HIS332
|
2.1
|
15.2
|
1.0
|
NE2
|
B:HIS372
|
2.1
|
15.5
|
1.0
|
O1
|
B:PER703
|
2.3
|
20.5
|
0.8
|
CE1
|
B:HIS328
|
2.9
|
16.5
|
1.0
|
CD2
|
B:HIS328
|
2.9
|
14.7
|
1.0
|
CE1
|
B:HIS372
|
3.0
|
14.1
|
1.0
|
CD2
|
B:HIS332
|
3.0
|
13.4
|
1.0
|
CE1
|
B:HIS332
|
3.0
|
14.4
|
1.0
|
CD2
|
B:HIS372
|
3.2
|
17.2
|
1.0
|
CU
|
B:CU701
|
3.5
|
16.1
|
0.7
|
CE2
|
B:PHE368
|
4.0
|
15.1
|
1.0
|
CE2
|
B:PHE513
|
4.0
|
15.8
|
1.0
|
ND1
|
B:HIS328
|
4.0
|
15.8
|
1.0
|
CG
|
B:HIS328
|
4.1
|
15.7
|
1.0
|
ND1
|
B:HIS372
|
4.1
|
14.2
|
1.0
|
ND1
|
B:HIS332
|
4.1
|
13.6
|
1.0
|
CG
|
B:HIS332
|
4.2
|
11.6
|
1.0
|
CG
|
B:HIS372
|
4.2
|
14.0
|
1.0
|
CZ
|
B:PHE103
|
4.4
|
15.4
|
1.0
|
CZ
|
B:PHE513
|
4.4
|
15.3
|
1.0
|
CZ
|
B:PHE368
|
4.5
|
17.4
|
1.0
|
CE1
|
B:PHE103
|
4.5
|
15.2
|
1.0
|
CD2
|
B:PHE368
|
4.6
|
12.8
|
1.0
|
CD2
|
B:HIS371
|
4.6
|
14.4
|
1.0
|
NE2
|
B:HIS67
|
4.8
|
13.9
|
1.0
|
CE1
|
B:PHE99
|
4.8
|
13.3
|
1.0
|
CD2
|
B:PHE513
|
4.9
|
15.4
|
1.0
|
NE2
|
B:HIS371
|
4.9
|
13.5
|
1.0
|
CE2
|
B:PHE103
|
5.0
|
15.1
|
1.0
|
|
Reference:
N.Fujieda,
K.Umakoshi,
Y.Ochi,
Y.Nishikawa,
S.Yanagisawa,
M.Kubo,
G.Kurisu,
S.Itoh.
Copper-Oxygen Dynamics in Tyrosinase Mechanism. Angew.Chem.Int.Ed.Engl. 2020.
ISSN: ESSN 1521-3773
PubMed: 32356371
DOI: 10.1002/ANIE.202004733
Page generated: Wed Jul 31 06:22:57 2024
|