Copper in PDB 4z11: Latent Aurone Synthase (Polyphenol Oxidase) From Natural Source
Protein crystallography data
The structure of Latent Aurone Synthase (Polyphenol Oxidase) From Natural Source, PDB code: 4z11
was solved by
C.Molitor,
S.G.Mauracher,
A.Rompel,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
46.38 /
2.50
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
62.570,
174.100,
102.540,
90.00,
105.27,
90.00
|
R / Rfree (%)
|
18.3 /
23.4
|
Copper Binding Sites:
The binding sites of Copper atom in the Latent Aurone Synthase (Polyphenol Oxidase) From Natural Source
(pdb code 4z11). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 8 binding sites of Copper where determined in the
Latent Aurone Synthase (Polyphenol Oxidase) From Natural Source, PDB code: 4z11:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Copper binding site 1 out
of 8 in 4z11
Go back to
Copper Binding Sites List in 4z11
Copper binding site 1 out
of 8 in the Latent Aurone Synthase (Polyphenol Oxidase) From Natural Source
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Latent Aurone Synthase (Polyphenol Oxidase) From Natural Source within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu700
b:46.7
occ:1.00
|
NE2
|
A:HIS125
|
2.0
|
40.8
|
1.0
|
NE2
|
A:HIS93
|
2.0
|
45.6
|
1.0
|
NE2
|
A:HIS116
|
2.1
|
41.6
|
1.0
|
O
|
A:HOH922
|
2.3
|
30.6
|
1.0
|
CE1
|
A:HIS125
|
2.8
|
39.0
|
1.0
|
HE1
|
A:HIS125
|
2.8
|
46.8
|
1.0
|
CE1
|
A:HIS116
|
2.9
|
40.3
|
1.0
|
CD2
|
A:HIS93
|
2.9
|
44.7
|
1.0
|
HD2
|
A:HIS93
|
3.1
|
53.6
|
1.0
|
CE1
|
A:HIS93
|
3.1
|
42.3
|
1.0
|
CD2
|
A:HIS116
|
3.1
|
44.4
|
1.0
|
CD2
|
A:HIS125
|
3.2
|
40.5
|
1.0
|
HE1
|
A:HIS93
|
3.3
|
50.8
|
1.0
|
HD11
|
A:ILE115
|
3.4
|
58.8
|
1.0
|
HD2
|
A:HIS116
|
3.4
|
53.3
|
1.0
|
HE1
|
A:HIS286
|
3.5
|
62.5
|
1.0
|
SG
|
A:CYS97
|
3.5
|
50.7
|
1.0
|
HD2
|
A:HIS125
|
3.5
|
48.6
|
1.0
|
HZ
|
A:PHE282
|
3.7
|
47.6
|
1.0
|
ND1
|
A:HIS125
|
4.0
|
39.7
|
1.0
|
CU
|
A:CU701
|
4.0
|
54.7
|
1.0
|
CE1
|
A:HIS286
|
4.0
|
52.0
|
1.0
|
HE1
|
A:PHE282
|
4.1
|
47.0
|
1.0
|
ND1
|
A:HIS116
|
4.1
|
41.2
|
1.0
|
CG
|
A:HIS93
|
4.1
|
42.6
|
1.0
|
ND1
|
A:HIS93
|
4.1
|
41.0
|
1.0
|
CG
|
A:HIS116
|
4.2
|
45.0
|
1.0
|
CG
|
A:HIS125
|
4.2
|
40.0
|
1.0
|
HD1
|
A:PHE273
|
4.2
|
61.0
|
1.0
|
NE2
|
A:HIS286
|
4.2
|
50.6
|
1.0
|
CD1
|
A:ILE115
|
4.3
|
49.0
|
1.0
|
HE1
|
A:PHE121
|
4.3
|
48.7
|
1.0
|
HE1
|
A:PHE273
|
4.3
|
65.4
|
1.0
|
HE2
|
A:PHE124
|
4.3
|
50.1
|
1.0
|
CD1
|
A:PHE273
|
4.4
|
50.9
|
1.0
|
HD13
|
A:ILE115
|
4.5
|
58.8
|
1.0
|
CE1
|
A:PHE273
|
4.5
|
54.5
|
1.0
|
CZ
|
A:PHE282
|
4.5
|
39.7
|
1.0
|
HD12
|
A:ILE115
|
4.6
|
58.8
|
1.0
|
CE1
|
A:PHE282
|
4.6
|
39.2
|
1.0
|
HD1
|
A:HIS125
|
4.7
|
47.7
|
1.0
|
HE1
|
A:HIS252
|
4.7
|
52.5
|
1.0
|
HD2
|
A:PHE124
|
4.7
|
50.8
|
1.0
|
HD1
|
A:HIS116
|
4.8
|
49.4
|
1.0
|
HD1
|
A:PHE121
|
4.9
|
46.6
|
1.0
|
HD1
|
A:HIS93
|
4.9
|
49.3
|
1.0
|
CE1
|
A:PHE121
|
5.0
|
40.6
|
1.0
|
ND1
|
A:HIS286
|
5.0
|
49.5
|
1.0
|
HB3
|
A:CYS97
|
5.0
|
51.1
|
1.0
|
|
Copper binding site 2 out
of 8 in 4z11
Go back to
Copper Binding Sites List in 4z11
Copper binding site 2 out
of 8 in the Latent Aurone Synthase (Polyphenol Oxidase) From Natural Source
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Latent Aurone Synthase (Polyphenol Oxidase) From Natural Source within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu701
b:54.7
occ:1.00
|
NE2
|
A:HIS286
|
2.0
|
50.6
|
1.0
|
NE2
|
A:HIS256
|
2.0
|
49.8
|
1.0
|
NE2
|
A:HIS252
|
2.0
|
47.1
|
1.0
|
O
|
A:HOH922
|
2.1
|
30.6
|
1.0
|
CE1
|
A:HIS286
|
2.6
|
52.0
|
1.0
|
HE1
|
A:HIS286
|
2.7
|
62.5
|
1.0
|
CE1
|
A:HIS252
|
2.8
|
43.7
|
1.0
|
CE1
|
A:HIS256
|
2.8
|
50.0
|
1.0
|
HE1
|
A:PHE282
|
2.9
|
47.0
|
1.0
|
HE1
|
A:HIS252
|
2.9
|
52.5
|
1.0
|
HE1
|
A:HIS256
|
3.0
|
59.9
|
1.0
|
CD2
|
A:HIS256
|
3.1
|
49.0
|
1.0
|
CD2
|
A:HIS252
|
3.1
|
45.4
|
1.0
|
CD2
|
A:HIS286
|
3.2
|
51.7
|
1.0
|
HD2
|
A:HIS256
|
3.3
|
58.9
|
1.0
|
HD2
|
A:HIS252
|
3.4
|
54.5
|
1.0
|
HD2
|
A:HIS286
|
3.6
|
62.1
|
1.0
|
CE1
|
A:PHE282
|
3.8
|
39.2
|
1.0
|
ND1
|
A:HIS286
|
3.8
|
49.5
|
1.0
|
HD2
|
A:HIS285
|
3.9
|
49.3
|
1.0
|
ND1
|
A:HIS252
|
4.0
|
43.9
|
1.0
|
ND1
|
A:HIS256
|
4.0
|
49.0
|
1.0
|
CU
|
A:CU700
|
4.0
|
46.7
|
1.0
|
HE1
|
A:PHE273
|
4.0
|
65.4
|
1.0
|
CG
|
A:HIS256
|
4.1
|
48.9
|
1.0
|
CG
|
A:HIS252
|
4.1
|
43.2
|
1.0
|
CG
|
A:HIS286
|
4.1
|
45.0
|
1.0
|
HE1
|
A:PHE121
|
4.1
|
48.7
|
1.0
|
HD1
|
A:PHE282
|
4.3
|
51.7
|
1.0
|
HE2
|
A:HIS285
|
4.5
|
47.4
|
1.0
|
CD1
|
A:PHE282
|
4.5
|
43.1
|
1.0
|
HD1
|
A:HIS286
|
4.6
|
59.4
|
1.0
|
HZ
|
A:PHE282
|
4.6
|
47.6
|
1.0
|
CD2
|
A:HIS285
|
4.6
|
41.0
|
1.0
|
CZ
|
A:PHE282
|
4.6
|
39.7
|
1.0
|
NE2
|
A:HIS93
|
4.6
|
45.6
|
1.0
|
HE1
|
A:HIS93
|
4.6
|
50.8
|
1.0
|
NE2
|
A:HIS125
|
4.7
|
40.8
|
1.0
|
HZ
|
A:PHE121
|
4.7
|
53.4
|
1.0
|
HD1
|
A:HIS252
|
4.7
|
52.7
|
1.0
|
HD1
|
A:HIS256
|
4.7
|
58.9
|
1.0
|
HD1
|
A:PHE273
|
4.8
|
61.0
|
1.0
|
NE2
|
A:HIS285
|
4.8
|
39.5
|
1.0
|
CE1
|
A:PHE273
|
4.9
|
54.5
|
1.0
|
CE1
|
A:PHE121
|
4.9
|
40.6
|
1.0
|
CE1
|
A:HIS93
|
4.9
|
42.3
|
1.0
|
|
Copper binding site 3 out
of 8 in 4z11
Go back to
Copper Binding Sites List in 4z11
Copper binding site 3 out
of 8 in the Latent Aurone Synthase (Polyphenol Oxidase) From Natural Source
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Latent Aurone Synthase (Polyphenol Oxidase) From Natural Source within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu700
b:46.1
occ:1.00
|
NE2
|
B:HIS93
|
2.0
|
42.0
|
1.0
|
NE2
|
B:HIS116
|
2.0
|
37.5
|
1.0
|
NE2
|
B:HIS125
|
2.0
|
35.8
|
1.0
|
O
|
B:HOH887
|
2.2
|
35.1
|
1.0
|
CE1
|
B:HIS125
|
2.7
|
34.2
|
1.0
|
HE1
|
B:HIS125
|
2.7
|
41.0
|
1.0
|
CE1
|
B:HIS116
|
2.8
|
38.5
|
1.0
|
CD2
|
B:HIS93
|
2.9
|
42.7
|
1.0
|
CE1
|
B:HIS93
|
3.0
|
43.1
|
1.0
|
HD2
|
B:HIS93
|
3.1
|
51.2
|
1.0
|
CD2
|
B:HIS116
|
3.1
|
37.5
|
1.0
|
HE1
|
B:HIS93
|
3.2
|
51.8
|
1.0
|
CD2
|
B:HIS125
|
3.2
|
33.8
|
1.0
|
HD11
|
B:ILE115
|
3.3
|
54.1
|
1.0
|
HD2
|
B:HIS116
|
3.4
|
44.9
|
1.0
|
SG
|
B:CYS97
|
3.5
|
46.4
|
1.0
|
HE1
|
B:HIS286
|
3.6
|
53.0
|
1.0
|
HD2
|
B:HIS125
|
3.6
|
40.5
|
1.0
|
HZ
|
B:PHE282
|
3.8
|
54.3
|
1.0
|
ND1
|
B:HIS125
|
3.9
|
33.6
|
1.0
|
ND1
|
B:HIS116
|
4.0
|
42.8
|
1.0
|
CG
|
B:HIS93
|
4.0
|
41.4
|
1.0
|
ND1
|
B:HIS93
|
4.0
|
42.3
|
1.0
|
CE1
|
B:HIS286
|
4.0
|
44.1
|
1.0
|
CU
|
B:CU701
|
4.0
|
47.9
|
1.0
|
CG
|
B:HIS116
|
4.2
|
38.7
|
1.0
|
HE1
|
B:PHE282
|
4.2
|
51.9
|
1.0
|
CG
|
B:HIS125
|
4.2
|
29.2
|
1.0
|
HE1
|
B:PHE121
|
4.2
|
45.4
|
1.0
|
HD1
|
B:PHE273
|
4.2
|
60.5
|
1.0
|
CD1
|
B:ILE115
|
4.2
|
45.1
|
1.0
|
NE2
|
B:HIS286
|
4.2
|
42.2
|
1.0
|
HE1
|
B:PHE273
|
4.2
|
60.0
|
1.0
|
CD1
|
B:PHE273
|
4.4
|
50.4
|
1.0
|
CE1
|
B:PHE273
|
4.4
|
50.0
|
1.0
|
HD13
|
B:ILE115
|
4.4
|
54.1
|
1.0
|
HE2
|
B:PHE124
|
4.5
|
51.0
|
1.0
|
HD12
|
B:ILE115
|
4.5
|
54.1
|
1.0
|
CZ
|
B:PHE282
|
4.6
|
45.2
|
1.0
|
HD1
|
B:HIS125
|
4.7
|
40.3
|
1.0
|
HD1
|
B:HIS116
|
4.7
|
51.3
|
1.0
|
CE1
|
B:PHE282
|
4.8
|
43.2
|
1.0
|
HD2
|
B:PHE124
|
4.8
|
49.8
|
1.0
|
HD1
|
B:HIS93
|
4.8
|
50.8
|
1.0
|
HE1
|
B:HIS252
|
4.9
|
50.6
|
1.0
|
HD1
|
B:PHE121
|
4.9
|
41.8
|
1.0
|
CE1
|
B:PHE121
|
4.9
|
37.8
|
1.0
|
CB
|
B:CYS97
|
5.0
|
48.1
|
1.0
|
|
Copper binding site 4 out
of 8 in 4z11
Go back to
Copper Binding Sites List in 4z11
Copper binding site 4 out
of 8 in the Latent Aurone Synthase (Polyphenol Oxidase) From Natural Source
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of Latent Aurone Synthase (Polyphenol Oxidase) From Natural Source within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu701
b:47.9
occ:1.00
|
NE2
|
B:HIS286
|
2.0
|
42.2
|
1.0
|
NE2
|
B:HIS256
|
2.0
|
43.4
|
1.0
|
NE2
|
B:HIS252
|
2.0
|
44.8
|
1.0
|
O
|
B:HOH887
|
2.1
|
35.1
|
1.0
|
CE1
|
B:HIS286
|
2.7
|
44.1
|
1.0
|
HE1
|
B:HIS286
|
2.7
|
53.0
|
1.0
|
CE1
|
B:HIS256
|
2.8
|
39.6
|
1.0
|
HE1
|
B:HIS256
|
3.0
|
47.6
|
1.0
|
CE1
|
B:HIS252
|
3.0
|
42.2
|
1.0
|
CD2
|
B:HIS252
|
3.0
|
43.4
|
1.0
|
HE1
|
B:PHE282
|
3.0
|
51.9
|
1.0
|
CD2
|
B:HIS256
|
3.0
|
45.2
|
1.0
|
CD2
|
B:HIS286
|
3.1
|
45.0
|
1.0
|
HD2
|
B:HIS252
|
3.2
|
52.1
|
1.0
|
HE1
|
B:HIS252
|
3.2
|
50.6
|
1.0
|
HD2
|
B:HIS256
|
3.3
|
54.3
|
1.0
|
HD2
|
B:HIS286
|
3.5
|
54.1
|
1.0
|
CE1
|
B:PHE282
|
3.8
|
43.2
|
1.0
|
HE1
|
B:PHE273
|
3.8
|
60.0
|
1.0
|
HD2
|
B:HIS285
|
3.9
|
46.4
|
1.0
|
ND1
|
B:HIS286
|
3.9
|
41.3
|
1.0
|
ND1
|
B:HIS256
|
3.9
|
39.1
|
1.0
|
CU
|
B:CU700
|
4.0
|
46.1
|
1.0
|
ND1
|
B:HIS252
|
4.1
|
42.0
|
1.0
|
CG
|
B:HIS256
|
4.1
|
42.6
|
1.0
|
CG
|
B:HIS252
|
4.1
|
41.3
|
1.0
|
CG
|
B:HIS286
|
4.1
|
42.7
|
1.0
|
HE1
|
B:PHE121
|
4.1
|
45.4
|
1.0
|
HD1
|
B:PHE282
|
4.4
|
53.9
|
1.0
|
HE2
|
B:HIS285
|
4.4
|
48.8
|
1.0
|
CD2
|
B:HIS285
|
4.5
|
38.7
|
1.0
|
CD1
|
B:PHE282
|
4.6
|
44.9
|
1.0
|
HE1
|
B:HIS93
|
4.6
|
51.8
|
1.0
|
HZ
|
B:PHE121
|
4.6
|
48.9
|
1.0
|
HD1
|
B:HIS286
|
4.6
|
49.5
|
1.0
|
NE2
|
B:HIS93
|
4.6
|
42.0
|
1.0
|
HZ
|
B:PHE282
|
4.6
|
54.3
|
1.0
|
CE1
|
B:PHE273
|
4.7
|
50.0
|
1.0
|
HD1
|
B:HIS256
|
4.7
|
46.9
|
1.0
|
CZ
|
B:PHE282
|
4.7
|
45.2
|
1.0
|
NE2
|
B:HIS125
|
4.7
|
35.8
|
1.0
|
HD1
|
B:PHE273
|
4.7
|
60.5
|
1.0
|
NE2
|
B:HIS285
|
4.8
|
40.6
|
1.0
|
HD12
|
B:ILE456
|
4.8
|
77.7
|
1.0
|
HD1
|
B:HIS252
|
4.8
|
50.4
|
1.0
|
CE1
|
B:HIS93
|
4.9
|
43.1
|
1.0
|
CE1
|
B:PHE121
|
4.9
|
37.8
|
1.0
|
|
Copper binding site 5 out
of 8 in 4z11
Go back to
Copper Binding Sites List in 4z11
Copper binding site 5 out
of 8 in the Latent Aurone Synthase (Polyphenol Oxidase) From Natural Source
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 5 of Latent Aurone Synthase (Polyphenol Oxidase) From Natural Source within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cu700
b:48.2
occ:1.00
|
NE2
|
C:HIS93
|
2.0
|
43.8
|
1.0
|
NE2
|
C:HIS116
|
2.0
|
46.1
|
1.0
|
NE2
|
C:HIS125
|
2.0
|
50.3
|
1.0
|
O
|
C:HOH891
|
2.2
|
31.1
|
1.0
|
CE1
|
C:HIS125
|
2.8
|
44.8
|
1.0
|
HE1
|
C:HIS125
|
2.8
|
53.7
|
1.0
|
CE1
|
C:HIS116
|
2.8
|
48.4
|
1.0
|
CD2
|
C:HIS93
|
2.9
|
44.5
|
1.0
|
HD2
|
C:HIS93
|
3.0
|
53.3
|
1.0
|
CE1
|
C:HIS93
|
3.0
|
44.5
|
1.0
|
CD2
|
C:HIS116
|
3.1
|
42.6
|
1.0
|
CD2
|
C:HIS125
|
3.2
|
49.3
|
1.0
|
HE1
|
C:HIS93
|
3.3
|
53.4
|
1.0
|
HD11
|
C:ILE115
|
3.3
|
56.5
|
1.0
|
HD2
|
C:HIS116
|
3.4
|
51.1
|
1.0
|
SG
|
C:CYS97
|
3.4
|
49.8
|
1.0
|
HD2
|
C:HIS125
|
3.6
|
59.2
|
1.0
|
HZ
|
C:PHE282
|
3.7
|
58.6
|
1.0
|
HE1
|
C:HIS286
|
3.7
|
65.1
|
1.0
|
ND1
|
C:HIS125
|
4.0
|
43.5
|
1.0
|
ND1
|
C:HIS116
|
4.0
|
46.6
|
1.0
|
CG
|
C:HIS93
|
4.0
|
42.7
|
1.0
|
ND1
|
C:HIS93
|
4.1
|
41.6
|
1.0
|
CU
|
C:CU701
|
4.1
|
57.7
|
1.0
|
CE1
|
C:HIS286
|
4.1
|
54.2
|
1.0
|
CG
|
C:HIS116
|
4.2
|
45.2
|
1.0
|
HE1
|
C:PHE121
|
4.2
|
48.8
|
1.0
|
HE1
|
C:PHE282
|
4.2
|
56.6
|
1.0
|
CD1
|
C:ILE115
|
4.2
|
47.1
|
1.0
|
CG
|
C:HIS125
|
4.2
|
47.6
|
1.0
|
NE2
|
C:HIS286
|
4.3
|
54.1
|
1.0
|
HD1
|
C:PHE273
|
4.3
|
62.1
|
1.0
|
HE2
|
C:PHE124
|
4.3
|
60.5
|
1.0
|
HD13
|
C:ILE115
|
4.4
|
56.5
|
1.0
|
HE1
|
C:PHE273
|
4.4
|
67.7
|
1.0
|
CD1
|
C:PHE273
|
4.4
|
51.8
|
1.0
|
HD12
|
C:ILE115
|
4.5
|
56.5
|
1.0
|
CZ
|
C:PHE282
|
4.5
|
48.8
|
1.0
|
CE1
|
C:PHE273
|
4.6
|
56.5
|
1.0
|
HD1
|
C:HIS125
|
4.7
|
52.2
|
1.0
|
HD2
|
C:PHE124
|
4.7
|
62.9
|
1.0
|
CE1
|
C:PHE282
|
4.7
|
47.2
|
1.0
|
HD1
|
C:HIS116
|
4.7
|
55.9
|
1.0
|
HD1
|
C:PHE121
|
4.8
|
46.3
|
1.0
|
HD1
|
C:HIS93
|
4.9
|
49.9
|
1.0
|
HE1
|
C:HIS252
|
4.9
|
58.5
|
1.0
|
CE1
|
C:PHE121
|
4.9
|
40.7
|
1.0
|
HB3
|
C:CYS97
|
4.9
|
51.2
|
1.0
|
CB
|
C:CYS97
|
4.9
|
42.7
|
1.0
|
|
Copper binding site 6 out
of 8 in 4z11
Go back to
Copper Binding Sites List in 4z11
Copper binding site 6 out
of 8 in the Latent Aurone Synthase (Polyphenol Oxidase) From Natural Source
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 6 of Latent Aurone Synthase (Polyphenol Oxidase) From Natural Source within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cu701
b:57.7
occ:1.00
|
NE2
|
C:HIS286
|
1.9
|
54.1
|
1.0
|
NE2
|
C:HIS256
|
1.9
|
51.7
|
1.0
|
NE2
|
C:HIS252
|
2.0
|
51.3
|
1.0
|
O
|
C:HOH891
|
2.2
|
31.1
|
1.0
|
CE1
|
C:HIS286
|
2.7
|
54.2
|
1.0
|
HE1
|
C:HIS286
|
2.7
|
65.1
|
1.0
|
CE1
|
C:HIS256
|
2.7
|
46.7
|
1.0
|
HE1
|
C:HIS256
|
2.8
|
56.1
|
1.0
|
HE1
|
C:PHE282
|
2.9
|
56.6
|
1.0
|
CE1
|
C:HIS252
|
3.0
|
48.8
|
1.0
|
CD2
|
C:HIS252
|
3.0
|
49.4
|
1.0
|
CD2
|
C:HIS256
|
3.1
|
50.7
|
1.0
|
CD2
|
C:HIS286
|
3.1
|
52.3
|
1.0
|
HE1
|
C:HIS252
|
3.2
|
58.5
|
1.0
|
HD2
|
C:HIS252
|
3.2
|
59.2
|
1.0
|
HD2
|
C:HIS256
|
3.4
|
60.9
|
1.0
|
HD2
|
C:HIS286
|
3.4
|
62.7
|
1.0
|
CE1
|
C:PHE282
|
3.7
|
47.2
|
1.0
|
HD2
|
C:HIS285
|
3.8
|
52.0
|
1.0
|
ND1
|
C:HIS286
|
3.9
|
50.2
|
1.0
|
ND1
|
C:HIS256
|
3.9
|
47.8
|
1.0
|
HE1
|
C:PHE273
|
4.0
|
67.7
|
1.0
|
ND1
|
C:HIS252
|
4.1
|
43.1
|
1.0
|
HE1
|
C:PHE121
|
4.1
|
48.8
|
1.0
|
CG
|
C:HIS286
|
4.1
|
49.2
|
1.0
|
CG
|
C:HIS256
|
4.1
|
48.6
|
1.0
|
CG
|
C:HIS252
|
4.1
|
45.7
|
1.0
|
CU
|
C:CU700
|
4.1
|
48.2
|
1.0
|
HD1
|
C:PHE282
|
4.3
|
59.8
|
1.0
|
HE2
|
C:HIS285
|
4.4
|
52.1
|
1.0
|
HZ
|
C:PHE121
|
4.5
|
51.6
|
1.0
|
CD2
|
C:HIS285
|
4.5
|
43.3
|
1.0
|
CD1
|
C:PHE282
|
4.5
|
49.8
|
1.0
|
HZ
|
C:PHE282
|
4.5
|
58.6
|
1.0
|
HD1
|
C:HIS286
|
4.6
|
60.2
|
1.0
|
CZ
|
C:PHE282
|
4.6
|
48.8
|
1.0
|
NE2
|
C:HIS125
|
4.6
|
50.3
|
1.0
|
HD1
|
C:HIS256
|
4.7
|
57.4
|
1.0
|
NE2
|
C:HIS93
|
4.7
|
43.8
|
1.0
|
HE1
|
C:HIS93
|
4.7
|
53.4
|
1.0
|
HD1
|
C:PHE273
|
4.7
|
62.1
|
1.0
|
NE2
|
C:HIS285
|
4.8
|
43.4
|
1.0
|
CE1
|
C:PHE121
|
4.8
|
40.7
|
1.0
|
CE1
|
C:PHE273
|
4.8
|
56.5
|
1.0
|
HD1
|
C:HIS252
|
4.8
|
51.7
|
1.0
|
CE1
|
C:HIS93
|
5.0
|
44.5
|
1.0
|
|
Copper binding site 7 out
of 8 in 4z11
Go back to
Copper Binding Sites List in 4z11
Copper binding site 7 out
of 8 in the Latent Aurone Synthase (Polyphenol Oxidase) From Natural Source
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 7 of Latent Aurone Synthase (Polyphenol Oxidase) From Natural Source within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cu700
b:47.6
occ:1.00
|
NE2
|
D:HIS93
|
1.9
|
50.4
|
1.0
|
NE2
|
D:HIS125
|
2.0
|
41.7
|
1.0
|
O
|
D:HOH851
|
2.1
|
39.0
|
1.0
|
NE2
|
D:HIS116
|
2.1
|
43.4
|
1.0
|
CE1
|
D:HIS125
|
2.8
|
43.2
|
1.0
|
HE1
|
D:HIS125
|
2.8
|
51.9
|
1.0
|
CD2
|
D:HIS93
|
2.8
|
49.8
|
1.0
|
CE1
|
D:HIS116
|
2.9
|
42.7
|
1.0
|
HD2
|
D:HIS93
|
2.9
|
59.8
|
1.0
|
CE1
|
D:HIS93
|
3.0
|
47.7
|
1.0
|
CD2
|
D:HIS116
|
3.1
|
45.1
|
1.0
|
CD2
|
D:HIS125
|
3.2
|
42.6
|
1.0
|
HE1
|
D:HIS93
|
3.3
|
57.2
|
1.0
|
HD11
|
D:ILE115
|
3.3
|
54.9
|
1.0
|
SG
|
D:CYS97
|
3.4
|
42.8
|
1.0
|
HD2
|
D:HIS116
|
3.4
|
54.2
|
1.0
|
HD2
|
D:HIS125
|
3.5
|
51.1
|
1.0
|
HE1
|
D:HIS286
|
3.7
|
54.5
|
1.0
|
HZ
|
D:PHE282
|
3.8
|
48.4
|
1.0
|
CG
|
D:HIS93
|
4.0
|
47.2
|
1.0
|
ND1
|
D:HIS125
|
4.0
|
43.8
|
1.0
|
ND1
|
D:HIS93
|
4.0
|
49.0
|
1.0
|
ND1
|
D:HIS116
|
4.1
|
43.0
|
1.0
|
CU
|
D:CU701
|
4.1
|
49.8
|
1.0
|
CE1
|
D:HIS286
|
4.1
|
45.4
|
1.0
|
CG
|
D:HIS116
|
4.2
|
41.6
|
1.0
|
CG
|
D:HIS125
|
4.2
|
40.0
|
1.0
|
HE1
|
D:PHE121
|
4.2
|
42.4
|
1.0
|
CD1
|
D:ILE115
|
4.2
|
45.8
|
1.0
|
HE1
|
D:PHE282
|
4.3
|
43.7
|
1.0
|
HE2
|
D:PHE124
|
4.3
|
57.9
|
1.0
|
HD1
|
D:PHE273
|
4.4
|
69.8
|
1.0
|
HD13
|
D:ILE115
|
4.4
|
54.9
|
1.0
|
NE2
|
D:HIS286
|
4.5
|
41.6
|
1.0
|
HE1
|
D:PHE273
|
4.5
|
66.2
|
1.0
|
HD12
|
D:ILE115
|
4.5
|
54.9
|
1.0
|
CD1
|
D:PHE273
|
4.6
|
58.1
|
1.0
|
CZ
|
D:PHE282
|
4.6
|
40.3
|
1.0
|
CE1
|
D:PHE273
|
4.6
|
55.2
|
1.0
|
HD2
|
D:PHE124
|
4.7
|
55.1
|
1.0
|
HD1
|
D:HIS125
|
4.7
|
52.5
|
1.0
|
HD1
|
D:HIS116
|
4.8
|
51.6
|
1.0
|
HD1
|
D:HIS93
|
4.8
|
58.8
|
1.0
|
CE1
|
D:PHE282
|
4.8
|
36.4
|
1.0
|
HD1
|
D:PHE121
|
4.9
|
41.9
|
1.0
|
CB
|
D:CYS97
|
4.9
|
33.4
|
1.0
|
HB3
|
D:CYS97
|
4.9
|
40.1
|
1.0
|
CE1
|
D:PHE121
|
4.9
|
35.4
|
1.0
|
|
Copper binding site 8 out
of 8 in 4z11
Go back to
Copper Binding Sites List in 4z11
Copper binding site 8 out
of 8 in the Latent Aurone Synthase (Polyphenol Oxidase) From Natural Source
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 8 of Latent Aurone Synthase (Polyphenol Oxidase) From Natural Source within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cu701
b:49.8
occ:1.00
|
HE2
|
D:HIS256
|
1.3
|
49.1
|
1.0
|
NE2
|
D:HIS286
|
1.9
|
41.6
|
1.0
|
NE2
|
D:HIS256
|
2.0
|
41.0
|
1.0
|
NE2
|
D:HIS252
|
2.1
|
40.2
|
1.0
|
O
|
D:HOH851
|
2.2
|
39.0
|
1.0
|
HE1
|
D:HIS286
|
2.5
|
54.5
|
1.0
|
CE1
|
D:HIS286
|
2.5
|
45.4
|
1.0
|
CE1
|
D:HIS256
|
2.8
|
40.5
|
1.0
|
HE1
|
D:HIS256
|
2.9
|
48.6
|
1.0
|
HE1
|
D:PHE282
|
2.9
|
43.7
|
1.0
|
CE1
|
D:HIS252
|
3.0
|
37.4
|
1.0
|
CD2
|
D:HIS256
|
3.1
|
39.2
|
1.0
|
CD2
|
D:HIS252
|
3.1
|
37.6
|
1.0
|
HE1
|
D:HIS252
|
3.1
|
44.8
|
1.0
|
CD2
|
D:HIS286
|
3.2
|
43.0
|
1.0
|
HD2
|
D:HIS252
|
3.3
|
45.1
|
1.0
|
HD2
|
D:HIS256
|
3.4
|
47.1
|
1.0
|
HD2
|
D:HIS286
|
3.6
|
51.7
|
1.0
|
ND1
|
D:HIS286
|
3.7
|
40.5
|
1.0
|
CE1
|
D:PHE282
|
3.8
|
36.4
|
1.0
|
ND1
|
D:HIS256
|
3.9
|
39.5
|
1.0
|
HD2
|
D:HIS285
|
4.0
|
56.5
|
1.0
|
HE1
|
D:PHE273
|
4.1
|
66.2
|
1.0
|
HE1
|
D:PHE121
|
4.1
|
42.4
|
1.0
|
CG
|
D:HIS286
|
4.1
|
38.9
|
1.0
|
ND1
|
D:HIS252
|
4.1
|
36.8
|
1.0
|
CG
|
D:HIS256
|
4.1
|
40.0
|
1.0
|
CU
|
D:CU700
|
4.1
|
47.6
|
1.0
|
CG
|
D:HIS252
|
4.2
|
40.5
|
1.0
|
HD1
|
D:PHE282
|
4.4
|
43.3
|
1.0
|
HD1
|
D:HIS286
|
4.4
|
48.6
|
1.0
|
HZ
|
D:PHE121
|
4.5
|
44.7
|
1.0
|
HE2
|
D:HIS285
|
4.5
|
49.7
|
1.0
|
HZ
|
D:PHE282
|
4.5
|
48.4
|
1.0
|
CD1
|
D:PHE282
|
4.5
|
36.1
|
1.0
|
NE2
|
D:HIS93
|
4.6
|
50.4
|
1.0
|
HE1
|
D:HIS93
|
4.6
|
57.2
|
1.0
|
NE2
|
D:HIS125
|
4.6
|
41.7
|
1.0
|
CZ
|
D:PHE282
|
4.6
|
40.3
|
1.0
|
CD2
|
D:HIS285
|
4.6
|
47.1
|
1.0
|
HD1
|
D:PHE273
|
4.8
|
69.8
|
1.0
|
CE1
|
D:PHE121
|
4.8
|
35.4
|
1.0
|
HD1
|
D:HIS252
|
4.8
|
44.2
|
1.0
|
CE1
|
D:PHE273
|
4.9
|
55.2
|
1.0
|
CE1
|
D:HIS93
|
4.9
|
47.7
|
1.0
|
NE2
|
D:HIS285
|
4.9
|
41.4
|
1.0
|
HD12
|
D:ILE456
|
4.9
|
52.8
|
1.0
|
|
Reference:
C.Molitor,
S.G.Mauracher,
A.Rompel.
Aurone Synthase Is A Catechol Oxidase with Hydroxylase Activity and Provides Insights Into the Mechanism of Plant Polyphenol Oxidases. Proc.Natl.Acad.Sci.Usa V. 113 E1806 2016.
ISSN: ESSN 1091-6490
PubMed: 26976571
DOI: 10.1073/PNAS.1523575113
Page generated: Wed Jul 31 03:42:42 2024
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