Copper in PDB 2zwe: Crystal Structure of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking the Deoxy-Form Crystal in Dioxygen-Saturated Solution For 40 Minutes
Enzymatic activity of Crystal Structure of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking the Deoxy-Form Crystal in Dioxygen-Saturated Solution For 40 Minutes
All present enzymatic activity of Crystal Structure of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking the Deoxy-Form Crystal in Dioxygen-Saturated Solution For 40 Minutes:
1.14.18.1;
Protein crystallography data
The structure of Crystal Structure of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking the Deoxy-Form Crystal in Dioxygen-Saturated Solution For 40 Minutes, PDB code: 2zwe
was solved by
Y.Matoba,
M.Sugiyama,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
30.00 /
1.32
|
Space group
|
P 21 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
65.240,
97.880,
55.090,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
17.4 /
20.8
|
Copper Binding Sites:
The binding sites of Copper atom in the Crystal Structure of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking the Deoxy-Form Crystal in Dioxygen-Saturated Solution For 40 Minutes
(pdb code 2zwe). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the
Crystal Structure of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking the Deoxy-Form Crystal in Dioxygen-Saturated Solution For 40 Minutes, PDB code: 2zwe:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
Copper binding site 1 out
of 6 in 2zwe
Go back to
Copper Binding Sites List in 2zwe
Copper binding site 1 out
of 6 in the Crystal Structure of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking the Deoxy-Form Crystal in Dioxygen-Saturated Solution For 40 Minutes
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 the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking the Deoxy-Form Crystal in Dioxygen-Saturated Solution For 40 Minutes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu501
b:30.3
occ:0.61
|
CU
|
A:CU501
|
0.0
|
30.3
|
0.6
|
NE2
|
A:HIS38
|
1.9
|
16.5
|
0.6
|
CU
|
A:CU501
|
2.0
|
17.5
|
0.4
|
O
|
B:HOH784
|
2.0
|
34.2
|
1.0
|
NE2
|
A:HIS54
|
2.1
|
21.5
|
1.0
|
O
|
B:HOH555
|
2.1
|
16.9
|
1.0
|
NE2
|
A:HIS38
|
2.5
|
15.0
|
0.4
|
NE2
|
A:HIS63
|
2.5
|
10.8
|
1.0
|
CE1
|
A:HIS38
|
2.6
|
16.1
|
0.6
|
CD2
|
A:HIS38
|
2.9
|
13.2
|
0.4
|
CD2
|
A:HIS54
|
3.0
|
20.6
|
1.0
|
CE1
|
A:HIS54
|
3.0
|
17.4
|
1.0
|
CE1
|
A:HIS63
|
3.1
|
8.5
|
1.0
|
CD2
|
A:HIS38
|
3.1
|
14.7
|
0.6
|
OE2
|
B:DAH98
|
3.5
|
10.2
|
0.3
|
CD2
|
A:HIS63
|
3.7
|
10.0
|
1.0
|
CE1
|
A:HIS38
|
3.7
|
13.0
|
0.4
|
CU
|
A:CU502
|
3.8
|
20.0
|
1.0
|
ND1
|
A:HIS38
|
3.8
|
13.0
|
0.6
|
OZ
|
B:DAH98
|
3.8
|
17.9
|
1.0
|
CG
|
A:HIS38
|
4.0
|
12.5
|
0.6
|
CG
|
A:HIS54
|
4.1
|
16.8
|
1.0
|
ND1
|
A:HIS54
|
4.1
|
15.8
|
1.0
|
NE2
|
A:HIS216
|
4.2
|
10.4
|
1.0
|
CG
|
A:HIS38
|
4.2
|
12.0
|
0.4
|
CE2
|
A:PHE212
|
4.3
|
11.5
|
1.0
|
CZ
|
A:PHE212
|
4.3
|
9.2
|
1.0
|
ND1
|
A:HIS63
|
4.3
|
8.5
|
1.0
|
CE1
|
A:HIS216
|
4.5
|
9.8
|
1.0
|
CG1
|
A:ILE42
|
4.5
|
35.4
|
1.0
|
ND1
|
A:HIS38
|
4.6
|
11.8
|
0.4
|
CG
|
A:HIS63
|
4.7
|
8.6
|
1.0
|
CE2
|
B:DAH98
|
4.7
|
13.6
|
1.0
|
CZ
|
B:DAH98
|
4.8
|
14.9
|
1.0
|
NE2
|
A:HIS190
|
4.9
|
9.7
|
1.0
|
CE1
|
A:PHE59
|
5.0
|
9.4
|
1.0
|
|
Copper binding site 2 out
of 6 in 2zwe
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Copper Binding Sites List in 2zwe
Copper binding site 2 out
of 6 in the Crystal Structure of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking the Deoxy-Form Crystal in Dioxygen-Saturated Solution For 40 Minutes
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 the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking the Deoxy-Form Crystal in Dioxygen-Saturated Solution For 40 Minutes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu501
b:17.5
occ:0.39
|
CU
|
A:CU501
|
0.0
|
17.5
|
0.4
|
CU
|
A:CU501
|
2.0
|
30.3
|
0.6
|
OZ
|
B:DAH98
|
2.0
|
17.9
|
1.0
|
OE2
|
B:DAH98
|
2.1
|
10.2
|
0.3
|
NE2
|
A:HIS38
|
2.2
|
15.0
|
0.4
|
O
|
B:HOH555
|
2.2
|
16.9
|
1.0
|
CE1
|
A:HIS38
|
2.3
|
16.1
|
0.6
|
NE2
|
A:HIS54
|
2.5
|
21.5
|
1.0
|
O
|
B:HOH784
|
2.6
|
34.2
|
1.0
|
NE2
|
A:HIS38
|
2.7
|
16.5
|
0.6
|
CE1
|
A:HIS38
|
2.8
|
13.0
|
0.4
|
CZ
|
B:DAH98
|
3.0
|
14.9
|
1.0
|
CE2
|
B:DAH98
|
3.1
|
13.6
|
1.0
|
CD2
|
A:HIS54
|
3.2
|
20.6
|
1.0
|
CG1
|
A:ILE42
|
3.4
|
35.4
|
1.0
|
CD2
|
A:HIS38
|
3.4
|
13.2
|
0.4
|
CD1
|
A:ILE42
|
3.4
|
35.3
|
1.0
|
ND1
|
A:HIS38
|
3.6
|
13.0
|
0.6
|
CE1
|
A:HIS54
|
3.6
|
17.4
|
1.0
|
CU
|
A:CU502
|
3.9
|
20.0
|
1.0
|
CD2
|
A:HIS38
|
4.1
|
14.7
|
0.6
|
ND1
|
A:HIS38
|
4.1
|
11.8
|
0.4
|
OG
|
A:SER206
|
4.2
|
10.0
|
1.0
|
CE1
|
B:DAH98
|
4.3
|
11.7
|
1.0
|
CG
|
A:HIS54
|
4.4
|
16.8
|
1.0
|
CG
|
A:HIS38
|
4.4
|
12.0
|
0.4
|
CD2
|
B:DAH98
|
4.4
|
12.3
|
1.0
|
CG
|
A:HIS38
|
4.5
|
12.5
|
0.6
|
NE2
|
A:HIS63
|
4.5
|
10.8
|
1.0
|
NE2
|
A:HIS194
|
4.5
|
8.1
|
1.0
|
ND1
|
A:HIS54
|
4.5
|
15.8
|
1.0
|
CE1
|
A:HIS194
|
4.6
|
8.3
|
1.0
|
O
|
B:HOH627
|
4.6
|
21.9
|
1.0
|
CE2
|
A:PHE212
|
4.6
|
11.5
|
1.0
|
CB
|
A:ILE42
|
4.8
|
22.2
|
1.0
|
CE1
|
A:HIS63
|
4.9
|
8.5
|
1.0
|
|
Copper binding site 3 out
of 6 in 2zwe
Go back to
Copper Binding Sites List in 2zwe
Copper binding site 3 out
of 6 in the Crystal Structure of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking the Deoxy-Form Crystal in Dioxygen-Saturated Solution For 40 Minutes
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 the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking the Deoxy-Form Crystal in Dioxygen-Saturated Solution For 40 Minutes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu502
b:20.0
occ:1.00
|
O
|
B:HOH555
|
1.9
|
16.9
|
1.0
|
NE2
|
A:HIS194
|
2.0
|
8.1
|
1.0
|
NE2
|
A:HIS190
|
2.0
|
9.7
|
1.0
|
NE2
|
A:HIS216
|
2.0
|
10.4
|
1.0
|
O
|
B:HOH784
|
2.7
|
34.2
|
1.0
|
CE1
|
A:HIS216
|
2.9
|
9.8
|
1.0
|
CE1
|
A:HIS194
|
2.9
|
8.3
|
1.0
|
CE1
|
A:HIS190
|
3.0
|
9.7
|
1.0
|
CD2
|
A:HIS190
|
3.0
|
10.1
|
1.0
|
CD2
|
A:HIS194
|
3.0
|
8.9
|
1.0
|
CD2
|
A:HIS216
|
3.1
|
10.8
|
1.0
|
OE2
|
B:DAH98
|
3.4
|
10.2
|
0.3
|
CU
|
A:CU501
|
3.8
|
30.3
|
0.6
|
CU
|
A:CU501
|
3.9
|
17.5
|
0.4
|
CE2
|
B:DAH98
|
4.0
|
13.6
|
1.0
|
ND1
|
A:HIS194
|
4.1
|
9.3
|
1.0
|
ND1
|
A:HIS216
|
4.1
|
9.7
|
1.0
|
OZ
|
B:DAH98
|
4.1
|
17.9
|
1.0
|
ND1
|
A:HIS190
|
4.1
|
9.2
|
1.0
|
CE2
|
A:PHE212
|
4.1
|
11.5
|
1.0
|
CG
|
A:HIS194
|
4.1
|
8.7
|
1.0
|
CG
|
A:HIS190
|
4.1
|
9.6
|
1.0
|
CG
|
A:HIS216
|
4.2
|
8.8
|
1.0
|
CD2
|
A:HIS215
|
4.3
|
11.5
|
1.0
|
CZ
|
B:DAH98
|
4.4
|
14.9
|
1.0
|
NE2
|
A:HIS215
|
4.5
|
10.7
|
1.0
|
NE2
|
A:HIS63
|
4.6
|
10.8
|
1.0
|
CD2
|
A:PHE212
|
4.7
|
8.5
|
1.0
|
CZ
|
A:PHE212
|
4.8
|
9.2
|
1.0
|
CD2
|
B:DAH98
|
4.8
|
12.3
|
1.0
|
CE1
|
A:PHE59
|
4.9
|
9.4
|
1.0
|
NE2
|
A:HIS38
|
5.0
|
16.5
|
0.6
|
|
Copper binding site 4 out
of 6 in 2zwe
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Copper Binding Sites List in 2zwe
Copper binding site 4 out
of 6 in the Crystal Structure of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking the Deoxy-Form Crystal in Dioxygen-Saturated Solution For 40 Minutes
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 the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking the Deoxy-Form Crystal in Dioxygen-Saturated Solution For 40 Minutes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu504
b:40.3
occ:0.50
|
NE2
|
A:HIS277
|
2.0
|
30.1
|
1.0
|
O
|
A:HOH939
|
2.4
|
29.3
|
0.5
|
CE1
|
A:HIS277
|
2.8
|
31.3
|
1.0
|
CD2
|
A:HIS277
|
3.1
|
32.6
|
1.0
|
ND1
|
A:HIS277
|
4.0
|
32.3
|
1.0
|
CG
|
A:HIS277
|
4.2
|
36.7
|
1.0
|
O
|
A:HOH934
|
4.4
|
54.6
|
1.0
|
CG
|
A:PRO231
|
4.6
|
22.7
|
1.0
|
O
|
A:HOH814
|
4.7
|
34.9
|
1.0
|
|
Copper binding site 5 out
of 6 in 2zwe
Go back to
Copper Binding Sites List in 2zwe
Copper binding site 5 out
of 6 in the Crystal Structure of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking the Deoxy-Form Crystal in Dioxygen-Saturated Solution For 40 Minutes
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 the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking the Deoxy-Form Crystal in Dioxygen-Saturated Solution For 40 Minutes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu503
b:18.2
occ:0.57
|
NE2
|
B:HIS82
|
2.0
|
12.8
|
0.6
|
NE2
|
B:HIS97
|
2.1
|
26.8
|
1.0
|
SD
|
B:MET84
|
2.2
|
26.1
|
1.0
|
CG
|
B:MET84
|
2.9
|
24.9
|
1.0
|
CE1
|
B:HIS82
|
3.0
|
15.5
|
0.6
|
CE1
|
B:HIS97
|
3.0
|
22.4
|
1.0
|
CD2
|
B:HIS82
|
3.1
|
14.5
|
0.6
|
CD2
|
B:HIS97
|
3.2
|
24.8
|
1.0
|
O
|
A:ILE42
|
3.3
|
16.7
|
1.0
|
CE
|
B:MET84
|
3.3
|
23.6
|
1.0
|
CE1
|
B:HIS82
|
3.4
|
15.5
|
0.4
|
ND1
|
B:HIS82
|
3.5
|
14.7
|
0.4
|
CB
|
B:MET84
|
3.6
|
14.7
|
1.0
|
CA
|
A:MET43
|
3.7
|
16.3
|
1.0
|
O
|
A:MET43
|
4.0
|
19.1
|
1.0
|
ND1
|
B:HIS82
|
4.1
|
15.3
|
0.6
|
C
|
A:MET43
|
4.1
|
15.4
|
1.0
|
ND1
|
B:HIS97
|
4.2
|
19.5
|
1.0
|
C
|
A:ILE42
|
4.2
|
17.8
|
1.0
|
CG
|
B:HIS82
|
4.2
|
12.1
|
0.6
|
CG
|
B:HIS97
|
4.3
|
15.7
|
1.0
|
N
|
A:MET43
|
4.4
|
13.5
|
1.0
|
O
|
A:HOH634
|
4.6
|
22.3
|
1.0
|
CB
|
A:MET43
|
4.6
|
17.1
|
1.0
|
NE2
|
B:HIS82
|
4.7
|
16.7
|
0.4
|
CA
|
B:MET84
|
4.8
|
13.8
|
1.0
|
CG
|
A:MET43
|
4.8
|
19.3
|
1.0
|
N
|
B:MET84
|
4.8
|
12.7
|
1.0
|
CG
|
B:HIS82
|
4.8
|
13.7
|
0.4
|
C
|
B:VAL83
|
5.0
|
12.1
|
1.0
|
|
Copper binding site 6 out
of 6 in 2zwe
Go back to
Copper Binding Sites List in 2zwe
Copper binding site 6 out
of 6 in the Crystal Structure of the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking the Deoxy-Form Crystal in Dioxygen-Saturated Solution For 40 Minutes
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 the Copper-Bound Tyrosinase in Complex with A Caddie Protein From Streptomyces Castaneoglobisporus Obtained By Soaking the Deoxy-Form Crystal in Dioxygen-Saturated Solution For 40 Minutes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu503
b:21.2
occ:0.43
|
OE1
|
B:GLU67
|
1.4
|
68.2
|
1.0
|
ND1
|
B:HIS68
|
1.8
|
54.2
|
1.0
|
NE2
|
B:HIS82
|
2.0
|
16.7
|
0.4
|
O
|
B:HIS68
|
2.2
|
55.4
|
1.0
|
N
|
B:HIS68
|
2.6
|
61.8
|
1.0
|
CD
|
B:GLU67
|
2.7
|
67.3
|
1.0
|
CE1
|
B:HIS68
|
2.7
|
55.4
|
1.0
|
C
|
B:HIS68
|
2.8
|
58.4
|
1.0
|
CG
|
B:HIS68
|
2.9
|
56.2
|
1.0
|
CD2
|
B:HIS82
|
3.0
|
16.0
|
0.4
|
CA
|
B:HIS68
|
3.0
|
59.7
|
1.0
|
CE1
|
B:HIS82
|
3.0
|
15.5
|
0.4
|
C
|
B:GLU67
|
3.3
|
64.5
|
1.0
|
CB
|
B:HIS68
|
3.4
|
57.8
|
1.0
|
OE2
|
B:GLU67
|
3.4
|
62.9
|
1.0
|
ND1
|
B:HIS82
|
3.5
|
15.3
|
0.6
|
CB
|
B:GLU67
|
3.5
|
67.3
|
1.0
|
CE1
|
B:HIS82
|
3.6
|
15.5
|
0.6
|
CG
|
B:GLU67
|
3.7
|
67.2
|
1.0
|
O
|
B:GLY69
|
3.8
|
69.9
|
1.0
|
NE2
|
B:HIS68
|
3.9
|
56.0
|
1.0
|
N
|
B:GLY69
|
3.9
|
60.8
|
1.0
|
CD2
|
B:HIS68
|
4.0
|
55.9
|
1.0
|
CA
|
B:GLU67
|
4.0
|
66.3
|
1.0
|
O
|
B:GLU67
|
4.0
|
67.7
|
1.0
|
O
|
A:MET43
|
4.1
|
19.1
|
1.0
|
ND1
|
B:HIS82
|
4.1
|
14.7
|
0.4
|
CG
|
B:HIS82
|
4.1
|
13.7
|
0.4
|
C
|
B:GLY69
|
4.2
|
61.6
|
1.0
|
CA
|
B:GLY69
|
4.6
|
62.4
|
1.0
|
O
|
B:HOH562
|
4.7
|
17.2
|
1.0
|
CG
|
B:HIS82
|
4.8
|
12.1
|
0.6
|
NE2
|
B:HIS82
|
4.9
|
12.8
|
0.6
|
N
|
B:GLY70
|
4.9
|
57.2
|
1.0
|
|
Reference:
Y.Matoba,
H.Yoshitsu,
H.J.Jeon,
K.Oda,
M.Noda,
T.Kumagai,
M.Sugiyama.
Crystallographic Evidence of Drastic Movement of A Copper Ion Toward the Substrate Tyrosine For Starting Hydroxylation Reaction of Tyrosinase To Be Published.
Page generated: Wed Jul 31 00:31:15 2024
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