Copper in PDB 2zwf: 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 80 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 80 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 80 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 80 Minutes, PDB code: 2zwf
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 /
1.40
|
Space group
|
P 21 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
65.160,
97.680,
54.990,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
17.3 /
21.2
|
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 80 Minutes
(pdb code 2zwf). 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 80 Minutes, PDB code: 2zwf:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
Copper binding site 1 out
of 6 in 2zwf
Go back to
Copper Binding Sites List in 2zwf
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 80 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 80 Minutes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu501
b:19.2
occ:0.63
|
CU
|
A:CU501
|
0.0
|
19.2
|
0.6
|
CU
|
A:CU501
|
1.8
|
16.1
|
0.4
|
O
|
B:HOH547
|
2.0
|
15.8
|
1.0
|
O
|
B:HOH582
|
2.0
|
19.2
|
1.0
|
NE2
|
A:HIS38
|
2.0
|
13.8
|
0.6
|
NE2
|
A:HIS54
|
2.1
|
19.8
|
1.0
|
NE2
|
A:HIS63
|
2.6
|
11.3
|
1.0
|
NE2
|
A:HIS38
|
2.6
|
13.5
|
0.4
|
CE1
|
A:HIS38
|
2.9
|
13.6
|
0.6
|
CD2
|
A:HIS54
|
2.9
|
18.9
|
1.0
|
CD2
|
A:HIS38
|
3.1
|
11.9
|
0.4
|
CD2
|
A:HIS38
|
3.1
|
11.7
|
0.6
|
CE1
|
A:HIS54
|
3.1
|
14.6
|
1.0
|
OE2
|
B:DAH98
|
3.2
|
14.9
|
0.4
|
CE1
|
A:HIS63
|
3.2
|
9.3
|
1.0
|
CU
|
A:CU502
|
3.5
|
18.0
|
1.0
|
OZ
|
B:DAH98
|
3.7
|
15.5
|
1.0
|
CD2
|
A:HIS63
|
3.7
|
10.7
|
1.0
|
CE1
|
A:HIS38
|
3.8
|
12.9
|
0.4
|
ND1
|
A:HIS38
|
4.0
|
12.7
|
0.6
|
CG
|
A:HIS54
|
4.1
|
14.3
|
1.0
|
NE2
|
A:HIS216
|
4.1
|
10.6
|
1.0
|
ND1
|
A:HIS54
|
4.2
|
14.7
|
1.0
|
CG
|
A:HIS38
|
4.2
|
11.5
|
0.6
|
CE2
|
A:PHE212
|
4.3
|
11.6
|
1.0
|
CZ
|
A:PHE212
|
4.4
|
10.4
|
1.0
|
CG
|
A:HIS38
|
4.4
|
11.0
|
0.4
|
CE2
|
B:DAH98
|
4.4
|
12.9
|
1.0
|
CE1
|
A:HIS216
|
4.4
|
11.5
|
1.0
|
ND1
|
A:HIS63
|
4.4
|
9.2
|
1.0
|
CZ
|
B:DAH98
|
4.6
|
15.5
|
1.0
|
CD1
|
A:ILE42
|
4.6
|
25.1
|
1.0
|
NE2
|
A:HIS190
|
4.7
|
8.9
|
1.0
|
ND1
|
A:HIS38
|
4.7
|
12.5
|
0.4
|
CG
|
A:HIS63
|
4.7
|
8.9
|
1.0
|
CE1
|
A:PHE59
|
4.9
|
7.5
|
1.0
|
NE2
|
A:HIS194
|
4.9
|
8.1
|
1.0
|
|
Copper binding site 2 out
of 6 in 2zwf
Go back to
Copper Binding Sites List in 2zwf
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 80 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 80 Minutes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu501
b:16.1
occ:0.37
|
CU
|
A:CU501
|
0.0
|
16.1
|
0.4
|
CU
|
A:CU501
|
1.8
|
19.2
|
0.6
|
O
|
B:HOH547
|
2.1
|
15.8
|
1.0
|
OZ
|
B:DAH98
|
2.1
|
15.5
|
1.0
|
NE2
|
A:HIS38
|
2.1
|
13.5
|
0.4
|
OE2
|
B:DAH98
|
2.1
|
14.9
|
0.4
|
CE1
|
A:HIS38
|
2.3
|
13.6
|
0.6
|
NE2
|
A:HIS38
|
2.4
|
13.8
|
0.6
|
NE2
|
A:HIS54
|
2.6
|
19.8
|
1.0
|
O
|
B:HOH582
|
2.6
|
19.2
|
1.0
|
CE1
|
A:HIS38
|
2.9
|
12.9
|
0.4
|
CZ
|
B:DAH98
|
3.0
|
15.5
|
1.0
|
CE2
|
B:DAH98
|
3.1
|
12.9
|
1.0
|
CD1
|
A:ILE42
|
3.2
|
25.1
|
1.0
|
CD2
|
A:HIS54
|
3.3
|
18.9
|
1.0
|
CD2
|
A:HIS38
|
3.3
|
11.9
|
0.4
|
ND1
|
A:HIS38
|
3.6
|
12.7
|
0.6
|
CE1
|
A:HIS54
|
3.6
|
14.6
|
1.0
|
CU
|
A:CU502
|
3.7
|
18.0
|
1.0
|
CD2
|
A:HIS38
|
3.8
|
11.7
|
0.6
|
CG1
|
A:ILE42
|
4.1
|
25.9
|
1.0
|
ND1
|
A:HIS38
|
4.1
|
12.5
|
0.4
|
OG
|
A:SER206
|
4.2
|
9.4
|
1.0
|
CG
|
A:HIS38
|
4.3
|
11.5
|
0.6
|
CG
|
A:HIS38
|
4.3
|
11.0
|
0.4
|
CE1
|
B:DAH98
|
4.4
|
11.4
|
1.0
|
NE2
|
A:HIS63
|
4.4
|
11.3
|
1.0
|
CD2
|
B:DAH98
|
4.4
|
10.2
|
1.0
|
CG
|
A:HIS54
|
4.4
|
14.3
|
1.0
|
NE2
|
A:HIS194
|
4.5
|
8.1
|
1.0
|
O
|
B:HOH556
|
4.5
|
16.4
|
1.0
|
CE1
|
A:HIS194
|
4.6
|
9.9
|
1.0
|
CE2
|
A:PHE212
|
4.6
|
11.6
|
1.0
|
ND1
|
A:HIS54
|
4.6
|
14.7
|
1.0
|
CB
|
A:ILE42
|
4.8
|
19.3
|
1.0
|
CE1
|
A:HIS63
|
4.9
|
9.3
|
1.0
|
NE2
|
A:HIS190
|
5.0
|
8.9
|
1.0
|
|
Copper binding site 3 out
of 6 in 2zwf
Go back to
Copper Binding Sites List in 2zwf
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 80 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 80 Minutes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu502
b:18.0
occ:1.00
|
NE2
|
A:HIS194
|
2.0
|
8.1
|
1.0
|
O
|
B:HOH547
|
2.0
|
15.8
|
1.0
|
NE2
|
A:HIS190
|
2.0
|
8.9
|
1.0
|
NE2
|
A:HIS216
|
2.1
|
10.6
|
1.0
|
O
|
B:HOH582
|
2.5
|
19.2
|
1.0
|
CE1
|
A:HIS216
|
2.9
|
11.5
|
1.0
|
CE1
|
A:HIS194
|
2.9
|
9.9
|
1.0
|
CE1
|
A:HIS190
|
2.9
|
10.2
|
1.0
|
CD2
|
A:HIS190
|
3.0
|
8.3
|
1.0
|
CD2
|
A:HIS194
|
3.0
|
10.2
|
1.0
|
OE2
|
B:DAH98
|
3.2
|
14.9
|
0.4
|
CD2
|
A:HIS216
|
3.2
|
10.0
|
1.0
|
CU
|
A:CU501
|
3.5
|
19.2
|
0.6
|
CU
|
A:CU501
|
3.7
|
16.1
|
0.4
|
CE2
|
B:DAH98
|
3.8
|
12.9
|
1.0
|
OZ
|
B:DAH98
|
4.0
|
15.5
|
1.0
|
ND1
|
A:HIS190
|
4.1
|
9.2
|
1.0
|
ND1
|
A:HIS194
|
4.1
|
9.8
|
1.0
|
ND1
|
A:HIS216
|
4.1
|
9.9
|
1.0
|
CG
|
A:HIS190
|
4.1
|
8.5
|
1.0
|
CG
|
A:HIS194
|
4.1
|
10.6
|
1.0
|
CE2
|
A:PHE212
|
4.2
|
11.6
|
1.0
|
CG
|
A:HIS216
|
4.2
|
8.7
|
1.0
|
CZ
|
B:DAH98
|
4.3
|
15.5
|
1.0
|
CD2
|
A:HIS215
|
4.5
|
11.3
|
1.0
|
NE2
|
A:HIS63
|
4.5
|
11.3
|
1.0
|
NE2
|
A:HIS215
|
4.6
|
10.7
|
1.0
|
CD2
|
B:DAH98
|
4.6
|
10.2
|
1.0
|
CZ
|
A:PHE212
|
4.8
|
10.4
|
1.0
|
CE1
|
A:PHE59
|
4.8
|
7.5
|
1.0
|
CD2
|
A:PHE212
|
4.9
|
8.9
|
1.0
|
NE2
|
A:HIS38
|
4.9
|
13.8
|
0.6
|
CD2
|
A:HIS63
|
5.0
|
10.7
|
1.0
|
|
Copper binding site 4 out
of 6 in 2zwf
Go back to
Copper Binding Sites List in 2zwf
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 80 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 80 Minutes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu504
b:45.4
occ:0.50
|
NE2
|
A:HIS277
|
2.0
|
52.1
|
1.0
|
O
|
A:HOH926
|
2.4
|
24.3
|
0.5
|
CE1
|
A:HIS277
|
2.8
|
51.9
|
1.0
|
O
|
A:HOH888
|
2.9
|
44.6
|
1.0
|
CD2
|
A:HIS277
|
3.1
|
54.7
|
1.0
|
ND1
|
A:HIS277
|
4.0
|
53.9
|
1.0
|
CG
|
A:HIS277
|
4.1
|
57.6
|
1.0
|
CG
|
A:PRO231
|
4.6
|
22.4
|
1.0
|
O
|
A:HOH733
|
4.8
|
30.8
|
1.0
|
|
Copper binding site 5 out
of 6 in 2zwf
Go back to
Copper Binding Sites List in 2zwf
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 80 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 80 Minutes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu503
b:17.9
occ:0.66
|
NE2
|
B:HIS82
|
2.0
|
13.4
|
0.7
|
NE2
|
B:HIS97
|
2.1
|
24.3
|
1.0
|
SD
|
B:MET84
|
2.3
|
24.3
|
1.0
|
CE1
|
B:HIS82
|
2.8
|
15.5
|
0.3
|
CE1
|
B:HIS97
|
2.9
|
23.7
|
1.0
|
CE1
|
B:HIS82
|
2.9
|
15.4
|
0.7
|
CD2
|
B:HIS82
|
3.1
|
15.9
|
0.7
|
CG
|
B:MET84
|
3.1
|
21.3
|
1.0
|
ND1
|
B:HIS82
|
3.2
|
14.6
|
0.3
|
O
|
A:ILE42
|
3.2
|
16.1
|
1.0
|
CD2
|
B:HIS97
|
3.2
|
21.3
|
1.0
|
CE
|
B:MET84
|
3.5
|
30.9
|
1.0
|
CB
|
B:MET84
|
3.7
|
13.5
|
1.0
|
CA
|
A:MET43
|
3.7
|
17.1
|
1.0
|
NE2
|
B:HIS82
|
4.0
|
15.5
|
0.3
|
ND1
|
B:HIS82
|
4.0
|
13.9
|
0.7
|
ND1
|
B:HIS97
|
4.1
|
18.3
|
1.0
|
O
|
A:MET43
|
4.1
|
21.4
|
1.0
|
C
|
A:ILE42
|
4.1
|
13.9
|
1.0
|
CG
|
B:HIS82
|
4.2
|
12.8
|
0.7
|
C
|
A:MET43
|
4.2
|
18.7
|
1.0
|
CG
|
B:HIS97
|
4.3
|
17.0
|
1.0
|
N
|
A:MET43
|
4.4
|
12.6
|
1.0
|
CG
|
B:HIS82
|
4.5
|
13.0
|
0.3
|
O
|
A:HOH576
|
4.6
|
18.4
|
1.0
|
CB
|
A:MET43
|
4.7
|
17.6
|
1.0
|
CG
|
A:MET43
|
4.8
|
19.8
|
1.0
|
CA
|
B:MET84
|
4.8
|
13.7
|
1.0
|
CD1
|
B:ILE92
|
4.8
|
36.7
|
1.0
|
N
|
B:MET84
|
4.9
|
12.2
|
1.0
|
CD2
|
B:HIS82
|
4.9
|
15.4
|
0.3
|
CG1
|
B:ILE92
|
5.0
|
14.9
|
1.0
|
|
Copper binding site 6 out
of 6 in 2zwf
Go back to
Copper Binding Sites List in 2zwf
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 80 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 80 Minutes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu503
b:24.5
occ:0.34
|
NE2
|
B:HIS82
|
2.6
|
15.5
|
0.3
|
CD2
|
B:HIS82
|
3.1
|
15.4
|
0.3
|
ND1
|
B:HIS82
|
3.7
|
13.9
|
0.7
|
CE1
|
B:HIS82
|
3.7
|
15.4
|
0.7
|
CE1
|
B:HIS82
|
3.8
|
15.5
|
0.3
|
O
|
A:MET43
|
3.9
|
21.4
|
1.0
|
CG
|
B:HIS82
|
4.4
|
13.0
|
0.3
|
O
|
B:HOH586
|
4.7
|
19.0
|
1.0
|
ND1
|
B:HIS82
|
4.7
|
14.6
|
0.3
|
CG
|
B:HIS82
|
5.0
|
12.8
|
0.7
|
|
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 00:31:37 2024
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