Copper in PDB 8ji8: Crystal Structure of Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti
Protein crystallography data
The structure of Crystal Structure of Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti, PDB code: 8ji8
was solved by
X.Zhu,
L.Zhang,
X.Yang,
P.Bao,
D.Ren,
Q.Han,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
47.69 /
2.65
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
91.57,
153.66,
223.17,
90,
90,
90
|
R / Rfree (%)
|
17.6 /
26.1
|
Copper Binding Sites:
The binding sites of Copper atom in the Crystal Structure of Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti
(pdb code 8ji8). 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 Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti, PDB code: 8ji8:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Copper binding site 1 out
of 8 in 8ji8
Go back to
Copper Binding Sites List in 8ji8
Copper binding site 1 out
of 8 in the Crystal Structure of Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti
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 Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu701
b:118.1
occ:1.00
|
NE2
|
A:HIS402
|
2.0
|
51.1
|
1.0
|
NE2
|
A:HIS366
|
2.1
|
47.2
|
1.0
|
NE2
|
A:HIS362
|
2.1
|
47.5
|
1.0
|
CD2
|
A:HIS366
|
2.7
|
37.7
|
1.0
|
CE1
|
A:HIS402
|
2.8
|
46.4
|
1.0
|
CD2
|
A:HIS362
|
2.8
|
38.7
|
1.0
|
CE1
|
A:HIS362
|
3.2
|
38.9
|
1.0
|
CD2
|
A:HIS402
|
3.2
|
40.6
|
1.0
|
CE1
|
A:HIS366
|
3.2
|
39.4
|
1.0
|
CG
|
A:HIS366
|
3.9
|
37.2
|
1.0
|
ND1
|
A:HIS402
|
4.0
|
43.5
|
1.0
|
CG
|
A:HIS362
|
4.0
|
38.1
|
1.0
|
ND1
|
A:HIS362
|
4.1
|
39.6
|
1.0
|
ND1
|
A:HIS366
|
4.1
|
38.5
|
1.0
|
CG
|
A:HIS402
|
4.2
|
38.0
|
1.0
|
CE2
|
A:PHE398
|
4.3
|
22.6
|
1.0
|
NE2
|
A:HIS235
|
4.3
|
87.9
|
1.0
|
CZ
|
A:PHE82
|
4.4
|
28.4
|
1.0
|
CE1
|
A:PHE82
|
4.5
|
27.3
|
1.0
|
CD1
|
A:TRP401
|
4.6
|
27.6
|
1.0
|
CD2
|
A:HIS235
|
4.6
|
59.8
|
1.0
|
CU
|
A:CU702
|
4.7
|
171.0
|
1.0
|
CZ
|
A:PHE398
|
4.7
|
22.7
|
1.0
|
NE1
|
A:TRP401
|
4.8
|
28.9
|
1.0
|
O
|
A:HIS362
|
4.9
|
35.4
|
1.0
|
CD2
|
A:PHE398
|
4.9
|
24.2
|
1.0
|
CE1
|
A:HIS235
|
4.9
|
77.7
|
1.0
|
|
Copper binding site 2 out
of 8 in 8ji8
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Copper Binding Sites List in 8ji8
Copper binding site 2 out
of 8 in the Crystal Structure of Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti
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 Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu702
b:171.0
occ:1.00
|
NE2
|
A:HIS206
|
2.1
|
66.2
|
1.0
|
NE2
|
A:HIS210
|
2.2
|
69.4
|
1.0
|
NE2
|
A:HIS235
|
2.2
|
87.9
|
1.0
|
CD2
|
A:HIS206
|
2.9
|
52.5
|
1.0
|
CE1
|
A:HIS235
|
2.9
|
77.7
|
1.0
|
CE1
|
A:HIS206
|
3.2
|
50.0
|
1.0
|
CE1
|
A:HIS210
|
3.2
|
56.5
|
1.0
|
CD2
|
A:HIS210
|
3.3
|
50.6
|
1.0
|
CD2
|
A:HIS235
|
3.5
|
59.8
|
1.0
|
CG
|
A:HIS206
|
4.1
|
45.7
|
1.0
|
ND1
|
A:HIS206
|
4.1
|
45.7
|
1.0
|
ND1
|
A:HIS235
|
4.2
|
60.3
|
1.0
|
CE
|
A:MET234
|
4.3
|
51.0
|
1.0
|
ND1
|
A:HIS210
|
4.4
|
40.1
|
1.0
|
CG
|
A:HIS210
|
4.5
|
41.7
|
1.0
|
CG
|
A:HIS235
|
4.5
|
47.6
|
1.0
|
CE1
|
A:HIS362
|
4.6
|
38.9
|
1.0
|
NE2
|
A:HIS362
|
4.6
|
47.5
|
1.0
|
CU
|
A:CU701
|
4.7
|
118.1
|
1.0
|
CE3
|
A:TRP209
|
4.7
|
32.1
|
1.0
|
|
Copper binding site 3 out
of 8 in 8ji8
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Copper Binding Sites List in 8ji8
Copper binding site 3 out
of 8 in the Crystal Structure of Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti
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 Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu701
b:116.2
occ:1.00
|
NE2
|
B:HIS402
|
2.1
|
54.0
|
1.0
|
NE2
|
B:HIS366
|
2.1
|
41.0
|
1.0
|
NE2
|
B:HIS362
|
2.1
|
47.5
|
1.0
|
CE1
|
B:HIS402
|
2.8
|
52.1
|
1.0
|
CD2
|
B:HIS366
|
2.8
|
33.6
|
1.0
|
CD2
|
B:HIS362
|
3.0
|
36.3
|
1.0
|
CE1
|
B:HIS366
|
3.1
|
34.5
|
1.0
|
CE1
|
B:HIS362
|
3.2
|
41.1
|
1.0
|
CD2
|
B:HIS402
|
3.3
|
43.6
|
1.0
|
CG
|
B:HIS366
|
3.9
|
33.8
|
1.0
|
ND1
|
B:HIS402
|
4.0
|
47.8
|
1.0
|
CE2
|
B:PHE398
|
4.0
|
25.2
|
1.0
|
ND1
|
B:HIS366
|
4.1
|
34.0
|
1.0
|
CG
|
B:HIS362
|
4.1
|
36.6
|
1.0
|
ND1
|
B:HIS362
|
4.2
|
40.6
|
1.0
|
NE2
|
B:HIS235
|
4.2
|
63.7
|
1.0
|
CE1
|
B:PHE82
|
4.2
|
27.3
|
1.0
|
CG
|
B:HIS402
|
4.3
|
42.5
|
1.0
|
CU
|
B:CU702
|
4.4
|
164.1
|
1.0
|
CZ
|
B:PHE82
|
4.4
|
28.0
|
1.0
|
CD2
|
B:HIS235
|
4.6
|
43.1
|
1.0
|
CZ
|
B:PHE398
|
4.6
|
24.1
|
1.0
|
CD2
|
B:PHE398
|
4.7
|
27.4
|
1.0
|
CD1
|
B:TRP401
|
4.8
|
31.4
|
1.0
|
CE1
|
B:HIS206
|
5.0
|
46.0
|
1.0
|
|
Copper binding site 4 out
of 8 in 8ji8
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Copper Binding Sites List in 8ji8
Copper binding site 4 out
of 8 in the Crystal Structure of Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti
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 Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu702
b:164.1
occ:1.00
|
NE2
|
B:HIS206
|
2.1
|
61.9
|
1.0
|
NE2
|
B:HIS210
|
2.2
|
73.9
|
1.0
|
NE2
|
B:HIS235
|
2.2
|
63.7
|
1.0
|
CE1
|
B:HIS235
|
2.9
|
53.9
|
1.0
|
CE1
|
B:HIS206
|
3.0
|
46.0
|
1.0
|
CD2
|
B:HIS206
|
3.1
|
49.1
|
1.0
|
CE1
|
B:HIS210
|
3.1
|
61.5
|
1.0
|
CD2
|
B:HIS210
|
3.3
|
49.5
|
1.0
|
CD2
|
B:HIS235
|
3.5
|
43.1
|
1.0
|
CE
|
B:MET234
|
3.9
|
51.1
|
1.0
|
ND1
|
B:HIS206
|
4.1
|
40.8
|
1.0
|
CG
|
B:HIS206
|
4.1
|
41.1
|
1.0
|
ND1
|
B:HIS235
|
4.1
|
41.7
|
1.0
|
ND1
|
B:HIS210
|
4.3
|
42.2
|
1.0
|
CU
|
B:CU701
|
4.4
|
116.2
|
1.0
|
CG
|
B:HIS210
|
4.5
|
41.0
|
1.0
|
CG
|
B:HIS235
|
4.5
|
40.4
|
1.0
|
CE1
|
B:HIS362
|
4.6
|
41.1
|
1.0
|
NE2
|
B:HIS362
|
4.6
|
47.5
|
1.0
|
CE2
|
B:PHE231
|
4.7
|
37.0
|
1.0
|
SD
|
B:MET234
|
5.0
|
55.3
|
1.0
|
|
Copper binding site 5 out
of 8 in 8ji8
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Copper Binding Sites List in 8ji8
Copper binding site 5 out
of 8 in the Crystal Structure of Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti
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 Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cu701
b:128.4
occ:1.00
|
NE2
|
C:HIS402
|
2.1
|
57.9
|
1.0
|
NE2
|
C:HIS366
|
2.1
|
49.4
|
1.0
|
NE2
|
C:HIS362
|
2.1
|
43.4
|
1.0
|
CE1
|
C:HIS402
|
2.7
|
48.0
|
1.0
|
CD2
|
C:HIS366
|
2.8
|
42.9
|
1.0
|
CD2
|
C:HIS362
|
2.9
|
36.0
|
1.0
|
CE1
|
C:HIS362
|
3.2
|
34.5
|
1.0
|
CE1
|
C:HIS366
|
3.2
|
40.2
|
1.0
|
CD2
|
C:HIS402
|
3.3
|
42.6
|
1.0
|
CG
|
C:HIS366
|
4.0
|
42.3
|
1.0
|
ND1
|
C:HIS402
|
4.0
|
46.8
|
1.0
|
CG
|
C:HIS362
|
4.0
|
34.5
|
1.0
|
ND1
|
C:HIS366
|
4.1
|
38.0
|
1.0
|
ND1
|
C:HIS362
|
4.1
|
36.3
|
1.0
|
CE2
|
C:PHE398
|
4.2
|
28.8
|
1.0
|
CZ
|
C:PHE82
|
4.2
|
31.1
|
1.0
|
CG
|
C:HIS402
|
4.2
|
41.1
|
1.0
|
CE1
|
C:PHE82
|
4.3
|
32.0
|
1.0
|
NE2
|
C:HIS235
|
4.3
|
64.6
|
1.0
|
CU
|
C:CU702
|
4.4
|
157.1
|
1.0
|
CZ
|
C:PHE398
|
4.6
|
28.0
|
1.0
|
CD2
|
C:HIS235
|
4.7
|
46.9
|
1.0
|
CD1
|
C:TRP401
|
4.8
|
33.8
|
1.0
|
CD2
|
C:PHE398
|
4.9
|
29.7
|
1.0
|
O
|
C:HIS362
|
4.9
|
36.8
|
1.0
|
CE1
|
C:HIS235
|
5.0
|
58.5
|
1.0
|
|
Copper binding site 6 out
of 8 in 8ji8
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Copper Binding Sites List in 8ji8
Copper binding site 6 out
of 8 in the Crystal Structure of Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti
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 Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cu702
b:157.1
occ:1.00
|
NE2
|
C:HIS206
|
2.1
|
62.0
|
1.0
|
NE2
|
C:HIS235
|
2.2
|
64.6
|
1.0
|
NE2
|
C:HIS210
|
2.2
|
67.0
|
1.0
|
CE1
|
C:HIS235
|
2.9
|
58.5
|
1.0
|
CD2
|
C:HIS206
|
3.0
|
48.2
|
1.0
|
CE1
|
C:HIS210
|
3.1
|
52.8
|
1.0
|
CE1
|
C:HIS206
|
3.1
|
54.4
|
1.0
|
CD2
|
C:HIS210
|
3.3
|
51.5
|
1.0
|
CD2
|
C:HIS235
|
3.4
|
46.9
|
1.0
|
CE
|
C:MET234
|
4.0
|
50.2
|
1.0
|
CG
|
C:HIS206
|
4.1
|
44.0
|
1.0
|
ND1
|
C:HIS235
|
4.2
|
51.0
|
1.0
|
ND1
|
C:HIS206
|
4.2
|
45.4
|
1.0
|
ND1
|
C:HIS210
|
4.3
|
44.9
|
1.0
|
CU
|
C:CU701
|
4.4
|
128.4
|
1.0
|
CG
|
C:HIS210
|
4.5
|
43.2
|
1.0
|
CG
|
C:HIS235
|
4.5
|
43.7
|
1.0
|
NE2
|
C:HIS362
|
4.7
|
43.4
|
1.0
|
CE1
|
C:HIS362
|
4.9
|
34.5
|
1.0
|
CE3
|
C:TRP209
|
4.9
|
38.0
|
1.0
|
|
Copper binding site 7 out
of 8 in 8ji8
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Copper Binding Sites List in 8ji8
Copper binding site 7 out
of 8 in the Crystal Structure of Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti
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 Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cu701
b:183.8
occ:1.00
|
NE2
|
D:HIS206
|
2.1
|
60.7
|
1.0
|
NE2
|
D:HIS210
|
2.2
|
84.1
|
1.0
|
NE2
|
D:HIS235
|
2.2
|
67.2
|
1.0
|
CE1
|
D:HIS235
|
2.8
|
52.4
|
1.0
|
CE1
|
D:HIS206
|
3.0
|
46.4
|
1.0
|
CD2
|
D:HIS206
|
3.1
|
46.0
|
1.0
|
CE1
|
D:HIS210
|
3.2
|
68.0
|
1.0
|
CD2
|
D:HIS210
|
3.3
|
60.5
|
1.0
|
CD2
|
D:HIS235
|
3.5
|
44.8
|
1.0
|
ND1
|
D:HIS206
|
4.0
|
43.1
|
1.0
|
CE
|
D:MET234
|
4.1
|
46.6
|
1.0
|
ND1
|
D:HIS235
|
4.1
|
46.5
|
1.0
|
CG
|
D:HIS206
|
4.1
|
41.0
|
1.0
|
CU
|
D:CU702
|
4.3
|
131.5
|
1.0
|
ND1
|
D:HIS210
|
4.3
|
55.4
|
1.0
|
CG
|
D:HIS210
|
4.4
|
53.1
|
1.0
|
CG
|
D:HIS235
|
4.5
|
42.8
|
1.0
|
NE2
|
D:HIS362
|
4.6
|
47.2
|
1.0
|
CE1
|
D:HIS362
|
4.8
|
38.6
|
1.0
|
SD
|
D:MET234
|
4.9
|
43.7
|
1.0
|
CZ
|
D:PHE398
|
5.0
|
26.8
|
1.0
|
|
Copper binding site 8 out
of 8 in 8ji8
Go back to
Copper Binding Sites List in 8ji8
Copper binding site 8 out
of 8 in the Crystal Structure of Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti
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 Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cu702
b:131.5
occ:1.00
|
NE2
|
D:HIS402
|
2.1
|
45.9
|
1.0
|
NE2
|
D:HIS366
|
2.1
|
45.9
|
1.0
|
NE2
|
D:HIS362
|
2.1
|
47.2
|
1.0
|
CE1
|
D:HIS402
|
2.7
|
41.2
|
1.0
|
CD2
|
D:HIS366
|
2.8
|
40.5
|
1.0
|
CD2
|
D:HIS362
|
2.9
|
35.8
|
1.0
|
CE1
|
D:HIS362
|
3.1
|
38.6
|
1.0
|
CE1
|
D:HIS366
|
3.3
|
36.5
|
1.0
|
CD2
|
D:HIS402
|
3.3
|
34.6
|
1.0
|
ND1
|
D:HIS402
|
4.0
|
40.8
|
1.0
|
CG
|
D:HIS366
|
4.0
|
38.8
|
1.0
|
CG
|
D:HIS362
|
4.0
|
35.3
|
1.0
|
NE2
|
D:HIS235
|
4.1
|
67.2
|
1.0
|
CE2
|
D:PHE398
|
4.1
|
25.9
|
1.0
|
ND1
|
D:HIS362
|
4.1
|
37.1
|
1.0
|
ND1
|
D:HIS366
|
4.2
|
37.9
|
1.0
|
CG
|
D:HIS402
|
4.2
|
34.9
|
1.0
|
CU
|
D:CU701
|
4.3
|
183.8
|
1.0
|
CZ
|
D:PHE82
|
4.5
|
27.7
|
1.0
|
CD2
|
D:HIS235
|
4.5
|
44.8
|
1.0
|
CE1
|
D:PHE82
|
4.5
|
30.6
|
1.0
|
CZ
|
D:PHE398
|
4.6
|
26.8
|
1.0
|
CE1
|
D:HIS235
|
4.7
|
52.4
|
1.0
|
CD1
|
D:TRP401
|
4.7
|
29.6
|
1.0
|
CD2
|
D:PHE398
|
4.8
|
24.4
|
1.0
|
O
|
D:HIS362
|
4.9
|
31.4
|
1.0
|
NE1
|
D:TRP401
|
4.9
|
27.8
|
1.0
|
NE2
|
D:HIS206
|
5.0
|
60.7
|
1.0
|
|
Reference:
X.Zhu,
L.Zhang,
H.Chen,
Y.Tang,
L.Jiang,
H.Ding,
X.Yang,
P.Bao,
C.Liao,
J.Li,
D.Ren,
C.J.Vavricka,
M.R.Strand,
Q.Han.
Mosquitoes Have Evolved Two Types of Prophenoloxidases To Be Published.
Page generated: Wed Jul 31 09:49:46 2024
|