Copper in PDB 3awt: Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 20 Hr: Occupancy of Cu(II) Is High
Enzymatic activity of Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 20 Hr: Occupancy of Cu(II) Is High
All present enzymatic activity of Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 20 Hr: Occupancy of Cu(II) Is High:
1.14.18.1;
Protein crystallography data
The structure of Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 20 Hr: Occupancy of Cu(II) Is High, PDB code: 3awt
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 (°)
|
65.150,
98.060,
55.090,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
17.5 /
20.9
|
Copper Binding Sites:
The binding sites of Copper atom in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 20 Hr: Occupancy of Cu(II) Is High
(pdb code 3awt). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 5 binding sites of Copper where determined in the
Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 20 Hr: Occupancy of Cu(II) Is High, PDB code: 3awt:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
Copper binding site 1 out
of 5 in 3awt
Go back to
Copper Binding Sites List in 3awt
Copper binding site 1 out
of 5 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 20 Hr: Occupancy of Cu(II) Is High
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 Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 20 Hr: Occupancy of Cu(II) Is High within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu500
b:19.2
occ:0.34
|
O
|
B:HOH624
|
2.0
|
21.1
|
1.0
|
NE2
|
A:HIS54
|
2.0
|
13.8
|
0.4
|
O
|
A:HOH511
|
2.2
|
25.2
|
0.8
|
NE2
|
A:HIS38
|
2.2
|
16.1
|
1.0
|
CE1
|
A:HIS38
|
2.4
|
13.0
|
1.0
|
NE2
|
A:HIS63
|
2.8
|
10.1
|
1.0
|
CD2
|
A:HIS54
|
2.9
|
14.4
|
0.4
|
CE1
|
A:HIS54
|
3.1
|
12.9
|
0.4
|
CE1
|
A:HIS63
|
3.2
|
8.3
|
1.0
|
CU
|
A:CU501
|
3.4
|
15.0
|
0.6
|
CD2
|
A:HIS38
|
3.6
|
16.1
|
1.0
|
OH
|
B:TYR98
|
3.7
|
26.4
|
1.0
|
ND1
|
A:HIS38
|
3.7
|
13.5
|
1.0
|
CD2
|
A:HIS63
|
4.0
|
9.1
|
1.0
|
CD1
|
A:ILE42
|
4.0
|
45.9
|
1.0
|
NE2
|
A:HIS216
|
4.1
|
12.1
|
1.0
|
CG
|
A:HIS54
|
4.1
|
12.0
|
0.4
|
ND1
|
A:HIS54
|
4.2
|
12.5
|
0.4
|
CG
|
A:HIS38
|
4.3
|
12.8
|
1.0
|
CE2
|
A:PHE212
|
4.4
|
10.1
|
1.0
|
CE1
|
A:HIS216
|
4.4
|
13.8
|
1.0
|
CZ
|
A:PHE212
|
4.5
|
9.5
|
1.0
|
ND1
|
A:HIS63
|
4.5
|
8.8
|
1.0
|
NE2
|
A:HIS190
|
4.7
|
11.8
|
1.0
|
CZ
|
B:TYR98
|
4.9
|
17.9
|
1.0
|
O
|
B:HOH512
|
4.9
|
12.3
|
0.6
|
CG
|
A:HIS63
|
4.9
|
9.1
|
1.0
|
CE1
|
A:PHE59
|
4.9
|
8.9
|
1.0
|
CB
|
A:HIS54
|
5.0
|
10.3
|
0.6
|
|
Copper binding site 2 out
of 5 in 3awt
Go back to
Copper Binding Sites List in 3awt
Copper binding site 2 out
of 5 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 20 Hr: Occupancy of Cu(II) Is High
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 Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 20 Hr: Occupancy of Cu(II) Is High within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu501
b:15.0
occ:0.55
|
O
|
B:HOH624
|
1.8
|
21.1
|
1.0
|
NE2
|
A:HIS190
|
2.0
|
11.8
|
1.0
|
NE2
|
A:HIS194
|
2.2
|
10.0
|
1.0
|
NE2
|
A:HIS216
|
2.3
|
12.1
|
1.0
|
O
|
A:HOH511
|
2.7
|
25.2
|
0.8
|
CE1
|
A:HIS190
|
2.9
|
10.8
|
1.0
|
CE1
|
A:HIS216
|
3.0
|
13.8
|
1.0
|
CD2
|
A:HIS190
|
3.0
|
10.3
|
1.0
|
CE1
|
A:HIS194
|
3.1
|
9.2
|
1.0
|
CD2
|
A:HIS194
|
3.1
|
10.4
|
1.0
|
CU
|
A:CU500
|
3.4
|
19.2
|
0.3
|
CD2
|
A:HIS216
|
3.4
|
13.0
|
1.0
|
OH
|
B:TYR98
|
3.9
|
26.4
|
1.0
|
ND1
|
A:HIS190
|
4.0
|
9.7
|
1.0
|
CG
|
A:HIS190
|
4.1
|
9.4
|
1.0
|
CE2
|
B:TYR98
|
4.2
|
16.0
|
1.0
|
ND1
|
A:HIS194
|
4.2
|
8.4
|
1.0
|
ND1
|
A:HIS216
|
4.2
|
10.8
|
1.0
|
CG
|
A:HIS194
|
4.3
|
9.3
|
1.0
|
CE2
|
A:PHE212
|
4.3
|
10.1
|
1.0
|
CZ
|
B:TYR98
|
4.3
|
17.9
|
1.0
|
CG
|
A:HIS216
|
4.4
|
10.6
|
1.0
|
CD2
|
A:HIS215
|
4.6
|
13.9
|
1.0
|
NE2
|
A:HIS63
|
4.6
|
10.1
|
1.0
|
NE2
|
A:HIS215
|
4.6
|
14.6
|
1.0
|
CE1
|
A:PHE59
|
4.7
|
8.9
|
1.0
|
CZ
|
A:PHE212
|
4.9
|
9.5
|
1.0
|
CE1
|
A:HIS38
|
5.0
|
13.0
|
1.0
|
CD2
|
A:PHE212
|
5.0
|
7.2
|
1.0
|
|
Copper binding site 3 out
of 5 in 3awt
Go back to
Copper Binding Sites List in 3awt
Copper binding site 3 out
of 5 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 20 Hr: Occupancy of Cu(II) Is High
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 Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 20 Hr: Occupancy of Cu(II) Is High within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu503
b:24.0
occ:0.50
|
NE2
|
A:HIS277
|
2.0
|
26.8
|
1.0
|
NE2
|
A:HIS279
|
2.2
|
41.1
|
1.0
|
CD2
|
A:HIS277
|
3.0
|
30.0
|
1.0
|
CE1
|
A:HIS277
|
3.0
|
24.7
|
1.0
|
CD2
|
A:HIS279
|
3.1
|
43.5
|
1.0
|
CE1
|
A:HIS279
|
3.3
|
42.6
|
1.0
|
ND1
|
A:HIS277
|
4.1
|
25.8
|
1.0
|
CG
|
A:HIS277
|
4.1
|
29.5
|
1.0
|
CG
|
A:HIS279
|
4.3
|
45.5
|
1.0
|
ND1
|
A:HIS279
|
4.4
|
43.2
|
1.0
|
O
|
A:HOH779
|
4.5
|
30.7
|
1.0
|
CG
|
A:PRO231
|
4.7
|
22.2
|
1.0
|
|
Copper binding site 4 out
of 5 in 3awt
Go back to
Copper Binding Sites List in 3awt
Copper binding site 4 out
of 5 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 20 Hr: Occupancy of Cu(II) Is High
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 Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 20 Hr: Occupancy of Cu(II) Is High within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu502
b:18.9
occ:0.82
|
OE1
|
B:GLU67
|
1.7
|
29.7
|
1.0
|
NE2
|
B:HIS82
|
2.0
|
22.0
|
1.0
|
ND1
|
B:HIS68
|
2.0
|
22.5
|
1.0
|
O
|
B:HIS68
|
2.1
|
28.8
|
1.0
|
N
|
B:HIS68
|
2.6
|
24.6
|
1.0
|
O
|
B:HOH851
|
2.8
|
37.0
|
1.0
|
C
|
B:HIS68
|
2.9
|
30.5
|
1.0
|
CE1
|
B:HIS68
|
2.9
|
23.2
|
1.0
|
CD
|
B:GLU67
|
2.9
|
33.6
|
1.0
|
CD2
|
B:HIS82
|
3.0
|
19.8
|
1.0
|
CE1
|
B:HIS82
|
3.0
|
18.9
|
1.0
|
CG
|
B:HIS68
|
3.1
|
22.8
|
1.0
|
CA
|
B:HIS68
|
3.1
|
24.1
|
1.0
|
C
|
B:GLU67
|
3.4
|
25.5
|
1.0
|
CB
|
B:GLU67
|
3.4
|
24.6
|
1.0
|
CB
|
B:HIS68
|
3.5
|
22.7
|
1.0
|
CG
|
B:GLU67
|
3.7
|
31.9
|
1.0
|
OE2
|
B:GLU67
|
3.9
|
31.5
|
1.0
|
CA
|
B:GLU67
|
4.0
|
25.0
|
1.0
|
NE2
|
B:HIS68
|
4.0
|
23.5
|
1.0
|
N
|
B:GLY69
|
4.1
|
38.4
|
1.0
|
ND1
|
B:HIS82
|
4.1
|
17.4
|
1.0
|
CD2
|
B:HIS68
|
4.1
|
20.8
|
1.0
|
CG
|
B:HIS82
|
4.1
|
16.9
|
1.0
|
O
|
B:GLU67
|
4.2
|
28.7
|
1.0
|
O
|
A:MET43
|
4.2
|
16.8
|
1.0
|
N
|
B:GLY70
|
4.4
|
49.7
|
1.0
|
O
|
B:HOH597
|
4.7
|
19.2
|
1.0
|
CA
|
B:GLY69
|
4.7
|
45.1
|
1.0
|
C
|
B:GLY69
|
4.9
|
50.6
|
1.0
|
|
Copper binding site 5 out
of 5 in 3awt
Go back to
Copper Binding Sites List in 3awt
Copper binding site 5 out
of 5 in the Crystal Structure of Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 20 Hr: Occupancy of Cu(II) Is High
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 Streptomyces Tyrosinase in A Complex with Caddie Soaked in A Cu(II)-Containing Solution For 20 Hr: Occupancy of Cu(II) Is High within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu502
b:18.9
occ:0.17
|
SD
|
B:MET84
|
1.4
|
47.2
|
0.4
|
CE
|
B:MET84
|
1.8
|
44.4
|
0.6
|
CE
|
B:MET84
|
2.1
|
26.4
|
0.4
|
CG
|
B:MET84
|
2.2
|
18.6
|
0.4
|
SD
|
B:MET84
|
2.7
|
27.1
|
0.6
|
N
|
B:NO3509
|
3.0
|
24.9
|
0.8
|
CB
|
B:MET84
|
3.0
|
16.8
|
0.6
|
O1
|
B:NO3509
|
3.0
|
32.4
|
0.8
|
CB
|
B:MET84
|
3.0
|
16.6
|
0.4
|
O3
|
B:NO3509
|
3.2
|
20.4
|
0.8
|
O
|
A:HOH510
|
3.4
|
25.4
|
0.8
|
CG
|
B:MET84
|
3.4
|
17.5
|
0.6
|
O2
|
B:NO3509
|
3.5
|
15.3
|
0.8
|
O
|
A:ILE42
|
3.5
|
16.4
|
1.0
|
O
|
A:MET43
|
3.7
|
16.8
|
1.0
|
CE1
|
B:HIS82
|
3.7
|
18.9
|
1.0
|
CE1
|
B:HIS97
|
3.9
|
17.1
|
1.0
|
CA
|
A:MET43
|
3.9
|
15.4
|
1.0
|
ND1
|
B:HIS82
|
4.0
|
17.4
|
1.0
|
C
|
A:MET43
|
4.1
|
16.3
|
1.0
|
ND1
|
B:HIS97
|
4.4
|
17.0
|
1.0
|
CA
|
B:MET84
|
4.4
|
12.8
|
1.0
|
C
|
A:ILE42
|
4.5
|
15.7
|
1.0
|
CD1
|
B:ILE92
|
4.7
|
16.6
|
1.0
|
O
|
A:ASP45
|
4.7
|
17.5
|
1.0
|
N
|
B:MET84
|
4.7
|
12.6
|
1.0
|
N
|
A:MET43
|
4.8
|
15.3
|
1.0
|
CG1
|
B:ILE92
|
4.9
|
12.0
|
1.0
|
CB
|
A:MET43
|
4.9
|
15.9
|
1.0
|
ND1
|
B:HIS68
|
5.0
|
22.5
|
1.0
|
NE2
|
B:HIS82
|
5.0
|
22.0
|
1.0
|
C
|
B:VAL83
|
5.0
|
13.4
|
1.0
|
|
Reference:
Y.Matoba,
N.Bando,
K.Oda,
M.Noda,
F.Higashikawa,
T.Kumagai,
M.Sugiyama.
A Molecular Mechanism For Copper Transportation to Tyrosinase That Is Assisted By A Metallochaperone, Caddie Protein J.Biol.Chem. V. 286 30219 2011.
ISSN: ISSN 0021-9258
PubMed: 21730070
DOI: 10.1074/JBC.M111.256818
Page generated: Wed Jul 31 00:42:19 2024
|