Copper in PDB 4a2f: Coriolopsis Gallica Laccase Collected at 12.65 Kev
Enzymatic activity of Coriolopsis Gallica Laccase Collected at 12.65 Kev
All present enzymatic activity of Coriolopsis Gallica Laccase Collected at 12.65 Kev:
1.10.3.2;
Protein crystallography data
The structure of Coriolopsis Gallica Laccase Collected at 12.65 Kev, PDB code: 4a2f
was solved by
E.De La Mora,
E.Rudino-Pinera,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
75.80 /
1.90
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
56.050,
85.500,
151.600,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
18.563 /
22.388
|
Copper Binding Sites:
The binding sites of Copper atom in the Coriolopsis Gallica Laccase Collected at 12.65 Kev
(pdb code 4a2f). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the
Coriolopsis Gallica Laccase Collected at 12.65 Kev, PDB code: 4a2f:
Jump to Copper binding site number:
1;
2;
3;
Copper binding site 1 out
of 3 in 4a2f
Go back to
Copper Binding Sites List in 4a2f
Copper binding site 1 out
of 3 in the Coriolopsis Gallica Laccase Collected at 12.65 Kev
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Coriolopsis Gallica Laccase Collected at 12.65 Kev within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu1518
b:23.3
occ:0.23
|
ND1
|
A:HIS415
|
2.1
|
31.6
|
1.0
|
ND1
|
A:HIS476
|
2.2
|
57.0
|
1.0
|
SG
|
A:CYS471
|
2.2
|
29.1
|
1.0
|
CD1
|
A:ILE473
|
2.9
|
32.7
|
1.0
|
CG
|
A:HIS415
|
2.9
|
28.4
|
1.0
|
CE1
|
A:HIS415
|
2.9
|
32.4
|
1.0
|
CG
|
A:HIS476
|
3.1
|
56.0
|
1.0
|
CE1
|
A:HIS476
|
3.2
|
58.1
|
1.0
|
CB
|
A:HIS415
|
3.3
|
23.5
|
1.0
|
CB
|
A:HIS476
|
3.3
|
54.7
|
1.0
|
CB
|
A:CYS471
|
3.5
|
30.3
|
1.0
|
CD2
|
A:PHE481
|
3.6
|
25.4
|
1.0
|
CB
|
A:ILE473
|
3.7
|
41.9
|
1.0
|
CG1
|
A:ILE473
|
3.8
|
40.7
|
1.0
|
CE2
|
A:PHE481
|
3.9
|
26.4
|
1.0
|
NE2
|
A:HIS415
|
3.9
|
33.2
|
1.0
|
CD2
|
A:HIS415
|
3.9
|
30.5
|
1.0
|
CA
|
A:HIS415
|
4.0
|
22.1
|
1.0
|
CD2
|
A:HIS476
|
4.3
|
58.2
|
1.0
|
NE2
|
A:HIS476
|
4.3
|
58.6
|
1.0
|
CG2
|
A:ILE473
|
4.6
|
42.4
|
1.0
|
CD
|
A:PRO416
|
4.6
|
17.0
|
1.0
|
CA
|
A:ILE473
|
4.7
|
42.4
|
1.0
|
N
|
A:ILE473
|
4.8
|
42.0
|
1.0
|
CA
|
A:CYS471
|
4.8
|
30.4
|
1.0
|
O
|
A:ILE473
|
4.8
|
41.3
|
1.0
|
CG
|
A:PHE481
|
4.8
|
25.8
|
1.0
|
O
|
A:GLY412
|
4.9
|
31.3
|
1.0
|
CA
|
A:HIS476
|
4.9
|
54.8
|
1.0
|
C
|
A:HIS415
|
5.0
|
20.1
|
1.0
|
|
Copper binding site 2 out
of 3 in 4a2f
Go back to
Copper Binding Sites List in 4a2f
Copper binding site 2 out
of 3 in the Coriolopsis Gallica Laccase Collected at 12.65 Kev
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Coriolopsis Gallica Laccase Collected at 12.65 Kev within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu1519
b:27.9
occ:0.54
|
NE2
|
A:HIS472
|
2.1
|
33.0
|
1.0
|
ND1
|
A:HIS87
|
2.2
|
27.5
|
1.0
|
O
|
A:HOH2147
|
2.5
|
38.8
|
1.0
|
NE2
|
A:HIS130
|
2.5
|
20.4
|
1.0
|
CE1
|
A:HIS472
|
3.1
|
35.4
|
1.0
|
CD2
|
A:HIS472
|
3.1
|
38.6
|
1.0
|
CE1
|
A:HIS87
|
3.1
|
26.7
|
1.0
|
CG
|
A:HIS87
|
3.2
|
19.6
|
1.0
|
CE1
|
A:HIS130
|
3.4
|
16.2
|
1.0
|
CB
|
A:HIS87
|
3.5
|
16.3
|
1.0
|
CD2
|
A:HIS130
|
3.5
|
21.0
|
1.0
|
CD2
|
A:HIS85
|
3.5
|
19.9
|
1.0
|
CZ2
|
A:TRP128
|
3.7
|
14.6
|
1.0
|
CD2
|
A:HIS418
|
4.0
|
25.5
|
0.8
|
NE2
|
A:HIS85
|
4.0
|
19.8
|
1.0
|
CE2
|
A:TRP128
|
4.0
|
16.6
|
1.0
|
CB
|
A:ALA261
|
4.1
|
13.7
|
1.0
|
NE1
|
A:TRP128
|
4.1
|
15.2
|
1.0
|
ND1
|
A:HIS472
|
4.2
|
34.8
|
1.0
|
CG
|
A:HIS472
|
4.2
|
40.1
|
1.0
|
NE2
|
A:HIS87
|
4.2
|
22.9
|
1.0
|
NE2
|
A:HIS418
|
4.2
|
25.9
|
0.8
|
NE2
|
A:HIS418
|
4.3
|
2.0
|
0.2
|
CD2
|
A:HIS87
|
4.3
|
22.2
|
1.0
|
O
|
A:HOH2380
|
4.4
|
36.2
|
1.0
|
CH2
|
A:TRP128
|
4.4
|
13.9
|
1.0
|
CD2
|
A:HIS418
|
4.5
|
6.2
|
0.2
|
CE1
|
A:HIS418
|
4.5
|
5.0
|
0.2
|
ND1
|
A:HIS130
|
4.5
|
21.4
|
1.0
|
CG
|
A:HIS130
|
4.6
|
15.9
|
1.0
|
CA
|
A:HIS87
|
4.6
|
16.4
|
1.0
|
CU
|
A:CU1520
|
4.7
|
29.9
|
0.8
|
CG
|
A:HIS85
|
4.8
|
20.6
|
1.0
|
CG
|
A:HIS418
|
4.9
|
23.0
|
0.8
|
CG
|
A:HIS418
|
4.9
|
10.9
|
0.2
|
ND1
|
A:HIS418
|
4.9
|
6.0
|
0.2
|
|
Copper binding site 3 out
of 3 in 4a2f
Go back to
Copper Binding Sites List in 4a2f
Copper binding site 3 out
of 3 in the Coriolopsis Gallica Laccase Collected at 12.65 Kev
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Coriolopsis Gallica Laccase Collected at 12.65 Kev within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu1520
b:29.9
occ:0.81
|
NE2
|
A:HIS420
|
2.0
|
15.1
|
1.0
|
NE2
|
A:HIS470
|
2.1
|
30.7
|
1.0
|
NE2
|
A:HIS418
|
2.1
|
2.0
|
0.2
|
NE2
|
A:HIS132
|
2.1
|
13.3
|
1.0
|
O
|
A:HOH2147
|
2.3
|
38.8
|
1.0
|
CE1
|
A:HIS470
|
2.8
|
34.8
|
1.0
|
CE1
|
A:HIS420
|
2.8
|
14.8
|
1.0
|
CE1
|
A:HIS418
|
3.0
|
5.0
|
0.2
|
CD2
|
A:HIS132
|
3.1
|
21.0
|
1.0
|
CD2
|
A:HIS418
|
3.1
|
6.2
|
0.2
|
CE1
|
A:HIS132
|
3.1
|
14.0
|
1.0
|
CD2
|
A:HIS420
|
3.2
|
17.8
|
1.0
|
CD2
|
A:HIS470
|
3.3
|
33.0
|
1.0
|
O
|
A:HOH2380
|
3.7
|
36.2
|
1.0
|
CD2
|
A:HIS418
|
3.9
|
25.5
|
0.8
|
ND1
|
A:HIS420
|
4.0
|
15.4
|
1.0
|
ND1
|
A:HIS470
|
4.0
|
32.4
|
1.0
|
ND1
|
A:HIS418
|
4.2
|
6.0
|
0.2
|
CG
|
A:HIS420
|
4.2
|
15.6
|
1.0
|
ND1
|
A:HIS132
|
4.2
|
13.9
|
1.0
|
CG
|
A:HIS418
|
4.2
|
10.9
|
0.2
|
CG
|
A:HIS470
|
4.3
|
28.7
|
1.0
|
CG
|
A:HIS132
|
4.3
|
19.0
|
1.0
|
CD2
|
A:PHE468
|
4.3
|
21.5
|
1.0
|
CD2
|
A:HIS85
|
4.6
|
19.9
|
1.0
|
CB
|
A:PHE468
|
4.6
|
17.6
|
1.0
|
NE2
|
A:HIS472
|
4.6
|
33.0
|
1.0
|
NE2
|
A:HIS418
|
4.7
|
25.9
|
0.8
|
CD2
|
A:HIS472
|
4.7
|
38.6
|
1.0
|
CG
|
A:PRO100
|
4.7
|
18.4
|
1.0
|
CU
|
A:CU1519
|
4.7
|
27.9
|
0.5
|
NE2
|
A:HIS85
|
4.8
|
19.8
|
1.0
|
CG
|
A:HIS418
|
4.8
|
23.0
|
0.8
|
CG
|
A:PHE468
|
4.9
|
18.4
|
1.0
|
|
Reference:
E.De La Mora,
J.E.Lovett,
C.F.Blanford,
E.F.Garman,
B.Valderrama,
E.Rudino-Pinera.
Structural Changes Caused By Radiation-Induced Reduction and Radiolysis: the Effect of X-Ray Absorbed Dose in A Fungal Multicopper Oxidase Acta Crystallogr.,Sect.D V. 68 564 2012.
ISSN: ISSN 0907-4449
PubMed: 22525754
DOI: 10.1107/S0907444912005343
Page generated: Wed Jul 31 02:31:18 2024
|