Copper in PDB 4a2h: Crystal Structure of Laccase From Coriolopsis Gallica pH 7.0
Enzymatic activity of Crystal Structure of Laccase From Coriolopsis Gallica pH 7.0
All present enzymatic activity of Crystal Structure of Laccase From Coriolopsis Gallica pH 7.0:
1.10.3.2;
Protein crystallography data
The structure of Crystal Structure of Laccase From Coriolopsis Gallica pH 7.0, PDB code: 4a2h
was solved by
E.De La Mora,
B.Valderrama,
E.Horjales,
E.Rudino-Pinera,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
34.26 /
2.30
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
56.470,
86.210,
152.240,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
18.9 /
22.5
|
Copper Binding Sites:
The binding sites of Copper atom in the Crystal Structure of Laccase From Coriolopsis Gallica pH 7.0
(pdb code 4a2h). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the
Crystal Structure of Laccase From Coriolopsis Gallica pH 7.0, PDB code: 4a2h:
Jump to Copper binding site number:
1;
2;
3;
4;
Copper binding site 1 out
of 4 in 4a2h
Go back to
Copper Binding Sites List in 4a2h
Copper binding site 1 out
of 4 in the Crystal Structure of Laccase From Coriolopsis Gallica pH 7.0
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 Laccase From Coriolopsis Gallica pH 7.0 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu1518
b:11.7
occ:0.34
|
ND1
|
A:HIS415
|
2.0
|
27.8
|
1.0
|
ND1
|
A:HIS476
|
2.1
|
40.1
|
1.0
|
SG
|
A:CYS471
|
2.1
|
30.6
|
1.0
|
CE1
|
A:HIS415
|
3.0
|
27.9
|
1.0
|
CG
|
A:HIS415
|
3.0
|
26.7
|
1.0
|
CE1
|
A:HIS476
|
3.1
|
40.6
|
1.0
|
CG
|
A:HIS476
|
3.1
|
39.5
|
1.0
|
CD1
|
A:ILE473
|
3.3
|
32.8
|
1.0
|
CB
|
A:CYS471
|
3.4
|
29.8
|
1.0
|
CB
|
A:HIS415
|
3.4
|
25.6
|
1.0
|
CB
|
A:HIS476
|
3.4
|
38.2
|
1.0
|
CD2
|
A:PHE481
|
3.7
|
27.8
|
1.0
|
CB
|
A:ILE473
|
3.8
|
35.1
|
1.0
|
CG1
|
A:ILE473
|
3.9
|
34.7
|
1.0
|
CA
|
A:HIS415
|
4.0
|
25.2
|
1.0
|
CE2
|
A:PHE481
|
4.0
|
28.1
|
1.0
|
NE2
|
A:HIS415
|
4.1
|
27.8
|
1.0
|
CD2
|
A:HIS415
|
4.1
|
26.5
|
1.0
|
NE2
|
A:HIS476
|
4.2
|
40.4
|
1.0
|
CD2
|
A:HIS476
|
4.3
|
39.5
|
1.0
|
CG2
|
A:ILE473
|
4.6
|
34.9
|
1.0
|
CD
|
A:PRO416
|
4.7
|
23.2
|
1.0
|
O
|
A:GLY412
|
4.7
|
31.8
|
1.0
|
CA
|
A:CYS471
|
4.7
|
30.0
|
1.0
|
N
|
A:ILE473
|
4.8
|
34.8
|
1.0
|
O
|
A:ILE473
|
4.8
|
35.8
|
1.0
|
CA
|
A:ILE473
|
4.8
|
35.3
|
1.0
|
N
|
A:HIS415
|
4.9
|
25.7
|
1.0
|
CG
|
A:PHE481
|
4.9
|
28.3
|
1.0
|
CA
|
A:HIS476
|
5.0
|
38.1
|
1.0
|
C
|
A:HIS415
|
5.0
|
24.5
|
1.0
|
|
Copper binding site 2 out
of 4 in 4a2h
Go back to
Copper Binding Sites List in 4a2h
Copper binding site 2 out
of 4 in the Crystal Structure of Laccase From Coriolopsis Gallica pH 7.0
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 Laccase From Coriolopsis Gallica pH 7.0 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu1519
b:26.5
occ:0.79
|
NE2
|
A:HIS470
|
1.9
|
30.2
|
1.0
|
NE2
|
A:HIS420
|
2.0
|
12.8
|
1.0
|
NE2
|
A:HIS132
|
2.0
|
18.4
|
1.0
|
O
|
A:HOH2093
|
2.1
|
41.3
|
1.0
|
CE1
|
A:HIS420
|
2.7
|
11.1
|
1.0
|
CE1
|
A:HIS470
|
2.7
|
32.2
|
1.0
|
CE1
|
A:HIS132
|
2.9
|
16.3
|
1.0
|
CD2
|
A:HIS470
|
3.0
|
29.8
|
1.0
|
CD2
|
A:HIS132
|
3.0
|
19.7
|
1.0
|
CD2
|
A:HIS420
|
3.2
|
13.9
|
1.0
|
ND1
|
A:HIS470
|
3.9
|
30.0
|
1.0
|
CD2
|
A:HIS418
|
3.9
|
23.1
|
1.0
|
ND1
|
A:HIS420
|
3.9
|
14.1
|
1.0
|
CG
|
A:HIS470
|
4.0
|
29.6
|
1.0
|
ND1
|
A:HIS132
|
4.1
|
18.1
|
1.0
|
CG
|
A:HIS132
|
4.1
|
19.1
|
1.0
|
CG
|
A:HIS420
|
4.2
|
16.8
|
1.0
|
CD2
|
A:PHE468
|
4.3
|
22.4
|
1.0
|
CD2
|
A:HIS85
|
4.4
|
22.6
|
1.0
|
CB
|
A:PHE468
|
4.5
|
20.4
|
1.0
|
CG
|
A:PRO100
|
4.5
|
18.4
|
1.0
|
CU
|
A:CU1521
|
4.6
|
96.6
|
1.0
|
NE2
|
A:HIS85
|
4.7
|
22.9
|
1.0
|
NE2
|
A:HIS472
|
4.7
|
32.0
|
1.0
|
NE2
|
A:HIS418
|
4.7
|
24.7
|
1.0
|
CU
|
A:CU1520
|
4.8
|
36.0
|
0.7
|
CG
|
A:PHE468
|
4.8
|
21.8
|
1.0
|
CD2
|
A:HIS472
|
4.9
|
32.2
|
1.0
|
CG
|
A:HIS418
|
4.9
|
21.9
|
1.0
|
|
Copper binding site 3 out
of 4 in 4a2h
Go back to
Copper Binding Sites List in 4a2h
Copper binding site 3 out
of 4 in the Crystal Structure of Laccase From Coriolopsis Gallica pH 7.0
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 Laccase From Coriolopsis Gallica pH 7.0 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu1520
b:36.0
occ:0.66
|
ND1
|
A:HIS87
|
2.0
|
18.8
|
1.0
|
NE2
|
A:HIS472
|
2.1
|
32.0
|
1.0
|
NE2
|
A:HIS130
|
2.3
|
21.9
|
1.0
|
O
|
A:HOH2093
|
2.8
|
41.3
|
1.0
|
CE1
|
A:HIS87
|
2.8
|
18.5
|
1.0
|
CE1
|
A:HIS472
|
3.0
|
32.2
|
1.0
|
CG
|
A:HIS87
|
3.2
|
19.7
|
1.0
|
CD2
|
A:HIS472
|
3.2
|
32.2
|
1.0
|
CD2
|
A:HIS130
|
3.2
|
21.5
|
1.0
|
CE1
|
A:HIS130
|
3.2
|
21.0
|
1.0
|
CD2
|
A:HIS85
|
3.6
|
22.6
|
1.0
|
CZ2
|
A:TRP128
|
3.7
|
15.4
|
1.0
|
CB
|
A:HIS87
|
3.7
|
19.1
|
1.0
|
CU
|
A:CU1521
|
4.0
|
96.6
|
1.0
|
NE2
|
A:HIS87
|
4.0
|
19.9
|
1.0
|
CE2
|
A:TRP128
|
4.0
|
17.5
|
1.0
|
NE2
|
A:HIS85
|
4.1
|
22.9
|
1.0
|
CD2
|
A:HIS418
|
4.1
|
23.1
|
1.0
|
ND1
|
A:HIS472
|
4.1
|
31.7
|
1.0
|
NE1
|
A:TRP128
|
4.2
|
18.6
|
1.0
|
CD2
|
A:HIS87
|
4.2
|
20.0
|
1.0
|
CG
|
A:HIS472
|
4.3
|
32.7
|
1.0
|
CB
|
A:ALA261
|
4.3
|
16.1
|
1.0
|
NE2
|
A:HIS418
|
4.3
|
24.7
|
1.0
|
ND1
|
A:HIS130
|
4.3
|
21.7
|
1.0
|
CG
|
A:HIS130
|
4.4
|
21.0
|
1.0
|
CH2
|
A:TRP128
|
4.4
|
16.8
|
1.0
|
CA
|
A:HIS87
|
4.8
|
19.5
|
1.0
|
CU
|
A:CU1519
|
4.8
|
26.5
|
0.8
|
CG
|
A:HIS85
|
4.8
|
22.1
|
1.0
|
CG
|
A:HIS418
|
5.0
|
21.9
|
1.0
|
|
Copper binding site 4 out
of 4 in 4a2h
Go back to
Copper Binding Sites List in 4a2h
Copper binding site 4 out
of 4 in the Crystal Structure of Laccase From Coriolopsis Gallica pH 7.0
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 Laccase From Coriolopsis Gallica pH 7.0 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu1521
b:96.6
occ:1.00
|
NE2
|
A:HIS418
|
1.8
|
24.7
|
1.0
|
NE2
|
A:HIS85
|
1.8
|
22.9
|
1.0
|
CE1
|
A:HIS85
|
2.7
|
21.0
|
1.0
|
CD2
|
A:HIS418
|
2.8
|
23.1
|
1.0
|
O
|
A:HOH2060
|
2.8
|
15.7
|
1.0
|
CE1
|
A:HIS418
|
2.8
|
23.9
|
1.0
|
CD2
|
A:HIS85
|
2.9
|
22.6
|
1.0
|
ND1
|
A:HIS87
|
3.3
|
18.8
|
1.0
|
CG
|
A:HIS87
|
3.5
|
19.7
|
1.0
|
CE1
|
A:HIS420
|
3.6
|
11.1
|
1.0
|
NE2
|
A:HIS420
|
3.6
|
12.8
|
1.0
|
CE1
|
A:HIS87
|
3.6
|
18.5
|
1.0
|
ND1
|
A:HIS420
|
3.7
|
14.1
|
1.0
|
CA
|
A:HIS87
|
3.8
|
19.5
|
1.0
|
CD2
|
A:HIS420
|
3.8
|
13.9
|
1.0
|
ND1
|
A:HIS85
|
3.8
|
22.2
|
1.0
|
ND1
|
A:HIS418
|
3.9
|
24.5
|
1.0
|
CG
|
A:HIS420
|
3.9
|
16.8
|
1.0
|
CG
|
A:HIS418
|
3.9
|
21.9
|
1.0
|
CD2
|
A:HIS87
|
3.9
|
20.0
|
1.0
|
CG
|
A:HIS85
|
4.0
|
22.1
|
1.0
|
NE2
|
A:HIS87
|
4.0
|
19.9
|
1.0
|
CU
|
A:CU1520
|
4.0
|
36.0
|
0.7
|
CB
|
A:HIS87
|
4.0
|
19.1
|
1.0
|
N
|
A:GLY88
|
4.0
|
19.6
|
1.0
|
O
|
A:HOH2093
|
4.2
|
41.3
|
1.0
|
C
|
A:HIS87
|
4.4
|
19.3
|
1.0
|
O
|
A:HOH2062
|
4.5
|
16.2
|
1.0
|
CU
|
A:CU1519
|
4.6
|
26.5
|
0.8
|
CA
|
A:HIS420
|
4.7
|
18.7
|
1.0
|
CB
|
A:HIS420
|
4.8
|
18.3
|
1.0
|
N
|
A:HIS87
|
4.8
|
19.6
|
1.0
|
O
|
A:HOH2261
|
4.8
|
22.8
|
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 02:31:34 2024
|