Copper in PDB 2zwd: 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 5 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 5 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 5 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 5 Minutes, PDB code: 2zwd
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 /
1.35
|
Space group
|
P 21 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
65.200,
97.830,
55.100,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
17.6 /
21.7
|
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 5 Minutes
(pdb code 2zwd). 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 5 Minutes, PDB code: 2zwd:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
Copper binding site 1 out
of 6 in 2zwd
Go back to
Copper Binding Sites List in 2zwd
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 5 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 5 Minutes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu502
b:19.1
occ:0.68
|
CU
|
A:CU1502
|
0.0
|
19.1
|
0.7
|
NE2
|
A:HIS38
|
1.8
|
13.9
|
0.7
|
NE2
|
A:HIS63
|
2.0
|
9.3
|
1.0
|
NE2
|
A:HIS54
|
2.1
|
21.6
|
1.0
|
NE2
|
A:HIS38
|
2.4
|
14.6
|
0.3
|
O
|
B:HOH545
|
2.5
|
14.8
|
1.0
|
CD2
|
A:HIS38
|
2.7
|
13.0
|
0.3
|
CU
|
A:CU1502
|
2.7
|
15.7
|
0.3
|
CE1
|
A:HIS63
|
2.7
|
11.3
|
1.0
|
CD2
|
A:HIS38
|
2.8
|
13.9
|
0.7
|
CE1
|
A:HIS38
|
2.9
|
14.5
|
0.7
|
CE1
|
A:HIS54
|
3.0
|
14.6
|
1.0
|
CD2
|
A:HIS54
|
3.2
|
21.4
|
1.0
|
CD2
|
A:HIS63
|
3.2
|
9.4
|
1.0
|
CE1
|
A:HIS38
|
3.7
|
13.9
|
0.3
|
CG
|
A:HIS38
|
3.9
|
11.4
|
0.7
|
ND1
|
A:HIS38
|
3.9
|
12.6
|
0.7
|
ND1
|
A:HIS63
|
3.9
|
9.3
|
1.0
|
CG
|
A:HIS38
|
4.0
|
11.6
|
0.3
|
CZ
|
A:PHE212
|
4.1
|
9.4
|
1.0
|
ND1
|
A:HIS54
|
4.1
|
15.9
|
1.0
|
CG
|
A:HIS54
|
4.2
|
16.5
|
1.0
|
CG
|
A:HIS63
|
4.2
|
8.6
|
1.0
|
CE2
|
A:PHE212
|
4.3
|
8.8
|
1.0
|
NE2
|
A:HIS216
|
4.3
|
9.6
|
1.0
|
CU
|
A:CU1503
|
4.3
|
15.1
|
1.0
|
CE1
|
A:HIS216
|
4.5
|
10.5
|
1.0
|
ND1
|
A:HIS38
|
4.5
|
11.7
|
0.3
|
CZ3
|
A:TRP62
|
4.5
|
9.7
|
1.0
|
OH
|
B:TYR98
|
4.6
|
14.5
|
1.0
|
CD1
|
A:ILE42
|
4.9
|
32.4
|
1.0
|
O
|
A:GLY53
|
4.9
|
10.8
|
1.0
|
CG1
|
A:ILE42
|
4.9
|
26.1
|
1.0
|
|
Copper binding site 2 out
of 6 in 2zwd
Go back to
Copper Binding Sites List in 2zwd
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 5 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 5 Minutes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu502
b:15.7
occ:0.32
|
CU
|
A:CU1502
|
0.0
|
15.7
|
0.3
|
O
|
B:HOH545
|
1.9
|
14.8
|
1.0
|
OH
|
B:TYR98
|
2.1
|
14.5
|
1.0
|
NE2
|
A:HIS38
|
2.3
|
14.6
|
0.3
|
CE1
|
A:HIS38
|
2.4
|
14.5
|
0.7
|
CU
|
A:CU1502
|
2.7
|
19.1
|
0.7
|
CE1
|
A:HIS38
|
2.8
|
13.9
|
0.3
|
NE2
|
A:HIS38
|
2.8
|
13.9
|
0.7
|
NE2
|
A:HIS54
|
2.8
|
21.6
|
1.0
|
CD1
|
A:ILE42
|
3.0
|
32.4
|
1.0
|
CZ
|
B:TYR98
|
3.1
|
14.4
|
1.0
|
CE2
|
B:TYR98
|
3.3
|
14.3
|
1.0
|
CD2
|
A:HIS54
|
3.4
|
21.4
|
1.0
|
CG1
|
A:ILE42
|
3.6
|
26.1
|
1.0
|
CD2
|
A:HIS38
|
3.6
|
13.0
|
0.3
|
ND1
|
A:HIS38
|
3.7
|
12.6
|
0.7
|
CE1
|
A:HIS54
|
3.8
|
14.6
|
1.0
|
CU
|
A:CU1503
|
4.0
|
15.1
|
1.0
|
ND1
|
A:HIS38
|
4.0
|
11.7
|
0.3
|
OG
|
A:SER206
|
4.1
|
10.3
|
1.0
|
CD2
|
A:HIS38
|
4.1
|
13.9
|
0.7
|
O
|
B:HOH796
|
4.3
|
31.6
|
1.0
|
CE1
|
B:TYR98
|
4.3
|
11.1
|
1.0
|
CG
|
A:HIS54
|
4.4
|
16.5
|
1.0
|
CG
|
A:HIS38
|
4.5
|
11.6
|
0.3
|
NE2
|
A:HIS194
|
4.5
|
9.4
|
1.0
|
NE2
|
A:HIS63
|
4.6
|
9.3
|
1.0
|
CG
|
A:HIS38
|
4.6
|
11.4
|
0.7
|
ND1
|
A:HIS54
|
4.6
|
15.9
|
1.0
|
CE1
|
A:HIS194
|
4.6
|
9.5
|
1.0
|
CD2
|
B:TYR98
|
4.6
|
12.9
|
1.0
|
CE2
|
A:PHE212
|
4.6
|
8.8
|
1.0
|
CE1
|
A:HIS190
|
5.0
|
8.8
|
1.0
|
|
Copper binding site 3 out
of 6 in 2zwd
Go back to
Copper Binding Sites List in 2zwd
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 5 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 5 Minutes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu503
b:15.1
occ:1.00
|
NE2
|
A:HIS194
|
2.0
|
9.4
|
1.0
|
NE2
|
A:HIS216
|
2.0
|
9.6
|
1.0
|
NE2
|
A:HIS190
|
2.0
|
8.5
|
1.0
|
O
|
B:HOH545
|
2.2
|
14.8
|
1.0
|
CE1
|
A:HIS216
|
2.9
|
10.5
|
1.0
|
CE1
|
A:HIS194
|
2.9
|
9.5
|
1.0
|
CE1
|
A:HIS190
|
3.0
|
8.8
|
1.0
|
CD2
|
A:HIS190
|
3.0
|
8.6
|
1.0
|
CD2
|
A:HIS194
|
3.0
|
9.5
|
1.0
|
CD2
|
A:HIS216
|
3.0
|
9.0
|
1.0
|
CE2
|
A:PHE212
|
4.0
|
8.8
|
1.0
|
CU
|
A:CU1502
|
4.0
|
15.7
|
0.3
|
ND1
|
A:HIS216
|
4.0
|
9.6
|
1.0
|
ND1
|
A:HIS194
|
4.0
|
10.4
|
1.0
|
CG
|
A:HIS216
|
4.1
|
8.1
|
1.0
|
ND1
|
A:HIS190
|
4.1
|
9.0
|
1.0
|
OH
|
B:TYR98
|
4.1
|
14.5
|
1.0
|
CD2
|
A:HIS215
|
4.1
|
10.9
|
1.0
|
CG
|
A:HIS194
|
4.1
|
8.6
|
1.0
|
CG
|
A:HIS190
|
4.1
|
8.4
|
1.0
|
CE2
|
B:TYR98
|
4.2
|
14.3
|
1.0
|
NE2
|
A:HIS215
|
4.3
|
11.8
|
1.0
|
CU
|
A:CU1502
|
4.3
|
19.1
|
0.7
|
CZ
|
B:TYR98
|
4.4
|
14.4
|
1.0
|
CD2
|
A:PHE212
|
4.6
|
7.1
|
1.0
|
CZ
|
A:PHE212
|
4.7
|
9.4
|
1.0
|
NE2
|
A:HIS63
|
4.8
|
9.3
|
1.0
|
|
Copper binding site 4 out
of 6 in 2zwd
Go back to
Copper Binding Sites List in 2zwd
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 5 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 5 Minutes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu504
b:39.5
occ:0.50
|
O
|
A:HOH819
|
2.1
|
32.5
|
1.0
|
O
|
A:HOH969
|
2.3
|
30.1
|
0.5
|
CG
|
A:PRO231
|
4.5
|
22.2
|
1.0
|
|
Copper binding site 5 out
of 6 in 2zwd
Go back to
Copper Binding Sites List in 2zwd
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 5 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 5 Minutes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu501
b:30.5
occ:0.47
|
NE2
|
B:HIS82
|
2.7
|
18.8
|
0.5
|
CD2
|
B:HIS82
|
3.2
|
19.5
|
0.5
|
ND1
|
B:HIS82
|
3.6
|
16.9
|
0.5
|
CE1
|
B:HIS82
|
3.7
|
17.4
|
0.5
|
CE1
|
B:HIS82
|
3.8
|
17.7
|
0.5
|
O
|
A:MET43
|
4.0
|
26.1
|
1.0
|
CG
|
B:HIS82
|
4.4
|
16.7
|
0.5
|
CE
|
B:MET84
|
4.5
|
21.4
|
0.5
|
ND1
|
B:HIS82
|
4.7
|
16.6
|
0.5
|
O
|
B:HOH592
|
4.8
|
18.6
|
1.0
|
CG
|
B:HIS82
|
4.9
|
15.9
|
0.5
|
O
|
B:VAL83
|
4.9
|
14.5
|
1.0
|
|
Copper binding site 6 out
of 6 in 2zwd
Go back to
Copper Binding Sites List in 2zwd
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 5 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 5 Minutes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu501
b:16.0
occ:0.53
|
O1
|
B:NO3505
|
1.3
|
18.9
|
0.5
|
NE2
|
B:HIS82
|
1.9
|
16.8
|
0.5
|
N
|
B:NO3505
|
2.0
|
18.5
|
0.5
|
SD
|
B:MET84
|
2.1
|
17.6
|
0.5
|
O2
|
B:NO3505
|
2.1
|
19.9
|
0.5
|
NE2
|
B:HIS97
|
2.2
|
19.8
|
0.5
|
CE
|
B:MET84
|
2.5
|
16.6
|
0.5
|
CE1
|
B:HIS82
|
2.6
|
17.7
|
0.5
|
CE1
|
B:HIS82
|
2.7
|
17.4
|
0.5
|
CG
|
B:MET84
|
2.7
|
18.8
|
0.5
|
CE1
|
B:HIS97
|
3.0
|
17.6
|
0.5
|
CD2
|
B:HIS82
|
3.1
|
15.6
|
0.5
|
O3
|
B:NO3505
|
3.1
|
29.5
|
0.5
|
ND1
|
B:HIS82
|
3.1
|
16.6
|
0.5
|
O
|
A:ILE42
|
3.3
|
15.0
|
1.0
|
CE
|
B:MET84
|
3.3
|
21.4
|
0.5
|
CD2
|
B:HIS97
|
3.3
|
18.0
|
0.5
|
SD
|
B:MET84
|
3.4
|
19.6
|
0.5
|
CB
|
B:MET84
|
3.5
|
16.4
|
1.0
|
CA
|
A:MET43
|
3.7
|
15.2
|
1.0
|
CE1
|
B:HIS97
|
3.7
|
16.9
|
0.5
|
NE2
|
B:HIS82
|
3.7
|
18.8
|
0.5
|
ND1
|
B:HIS82
|
3.8
|
16.9
|
0.5
|
ND1
|
B:HIS97
|
4.0
|
15.1
|
0.5
|
CG
|
B:MET84
|
4.1
|
21.7
|
0.5
|
CG
|
B:HIS82
|
4.1
|
15.9
|
0.5
|
C
|
A:ILE42
|
4.1
|
16.7
|
1.0
|
O
|
A:MET43
|
4.2
|
26.1
|
1.0
|
ND1
|
B:HIS97
|
4.2
|
14.6
|
0.5
|
C
|
A:MET43
|
4.2
|
17.6
|
1.0
|
N
|
A:MET43
|
4.3
|
14.9
|
1.0
|
CG
|
B:HIS97
|
4.4
|
15.0
|
0.5
|
CG
|
B:HIS82
|
4.4
|
16.7
|
0.5
|
CB
|
A:MET43
|
4.6
|
16.0
|
1.0
|
CG
|
A:MET43
|
4.6
|
18.5
|
1.0
|
CD2
|
B:HIS82
|
4.7
|
19.5
|
0.5
|
CA
|
B:MET84
|
4.7
|
13.7
|
1.0
|
O
|
A:HOH554
|
4.8
|
15.9
|
1.0
|
N
|
B:MET84
|
4.8
|
12.8
|
1.0
|
CG2
|
A:ILE42
|
4.8
|
24.9
|
1.0
|
C
|
B:VAL83
|
4.9
|
11.4
|
1.0
|
O
|
B:VAL83
|
4.9
|
14.5
|
1.0
|
NE2
|
B:HIS97
|
4.9
|
16.1
|
0.5
|
|
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 00:31:12 2024
|