Copper in PDB 2hrh: Crystal Structure of Blue Laccase From Trametes Trogii
Enzymatic activity of Crystal Structure of Blue Laccase From Trametes Trogii
All present enzymatic activity of Crystal Structure of Blue Laccase From Trametes Trogii:
1.10.3.2;
Protein crystallography data
The structure of Crystal Structure of Blue Laccase From Trametes Trogii, PDB code: 2hrh
was solved by
I.Matera,
A.Gullotto,
M.Ferraroni,
S.Tilli,
F.Briganti,
A.Scozzafava,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
39.53 /
2.60
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
84.932,
84.327,
108.383,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
17.5 /
23.3
|
Copper Binding Sites:
The binding sites of Copper atom in the Crystal Structure of Blue Laccase From Trametes Trogii
(pdb code 2hrh). 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 Blue Laccase From Trametes Trogii, PDB code: 2hrh:
Jump to Copper binding site number:
1;
2;
3;
4;
Copper binding site 1 out
of 4 in 2hrh
Go back to
Copper Binding Sites List in 2hrh
Copper binding site 1 out
of 4 in the Crystal Structure of Blue Laccase From Trametes Trogii
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 Blue Laccase From Trametes Trogii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu497
b:39.4
occ:1.00
|
ND1
|
A:HIS455
|
2.1
|
30.9
|
1.0
|
ND1
|
A:HIS394
|
2.1
|
28.5
|
1.0
|
SG
|
A:CYS450
|
2.1
|
28.1
|
1.0
|
CE1
|
A:HIS394
|
3.0
|
29.6
|
1.0
|
CG
|
A:HIS455
|
3.0
|
29.9
|
1.0
|
CE1
|
A:HIS455
|
3.1
|
28.8
|
1.0
|
CG
|
A:HIS394
|
3.1
|
25.4
|
1.0
|
CB
|
A:HIS455
|
3.3
|
30.0
|
1.0
|
CB
|
A:CYS450
|
3.5
|
25.2
|
1.0
|
CB
|
A:HIS394
|
3.5
|
24.7
|
1.0
|
CD1
|
A:ILE452
|
3.6
|
27.8
|
1.0
|
CB
|
A:ILE452
|
3.6
|
28.2
|
1.0
|
CD2
|
A:PHE460
|
3.7
|
24.9
|
1.0
|
CG1
|
A:ILE452
|
3.8
|
26.7
|
1.0
|
CE2
|
A:PHE460
|
3.9
|
25.0
|
1.0
|
CA
|
A:HIS394
|
4.0
|
24.9
|
1.0
|
NE2
|
A:HIS394
|
4.1
|
28.4
|
1.0
|
NE2
|
A:HIS455
|
4.2
|
29.2
|
1.0
|
CD2
|
A:HIS455
|
4.2
|
28.1
|
1.0
|
CD2
|
A:HIS394
|
4.2
|
27.8
|
1.0
|
CG2
|
A:ILE452
|
4.4
|
28.2
|
1.0
|
O
|
A:GLY391
|
4.4
|
31.4
|
1.0
|
N
|
A:ILE452
|
4.7
|
28.1
|
1.0
|
CA
|
A:ILE452
|
4.7
|
28.4
|
1.0
|
CA
|
A:CYS450
|
4.8
|
26.1
|
1.0
|
CD
|
A:PRO395
|
4.8
|
23.6
|
1.0
|
CA
|
A:HIS455
|
4.9
|
30.8
|
1.0
|
O
|
A:ILE452
|
4.9
|
28.3
|
1.0
|
C
|
A:HIS394
|
4.9
|
24.6
|
1.0
|
N
|
A:HIS394
|
5.0
|
25.1
|
1.0
|
|
Copper binding site 2 out
of 4 in 2hrh
Go back to
Copper Binding Sites List in 2hrh
Copper binding site 2 out
of 4 in the Crystal Structure of Blue Laccase From Trametes Trogii
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 Blue Laccase From Trametes Trogii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu498
b:59.5
occ:1.00
|
NE2
|
A:HIS397
|
1.8
|
31.0
|
1.0
|
NE2
|
A:HIS64
|
2.1
|
29.8
|
1.0
|
CE1
|
A:HIS397
|
2.8
|
28.8
|
1.0
|
CD2
|
A:HIS397
|
2.8
|
28.4
|
1.0
|
CD2
|
A:HIS64
|
3.0
|
25.0
|
1.0
|
CE1
|
A:HIS64
|
3.0
|
27.9
|
1.0
|
NE2
|
A:HIS399
|
3.3
|
28.0
|
1.0
|
CU
|
A:CU500
|
3.3
|
44.3
|
1.0
|
ND1
|
A:HIS66
|
3.4
|
21.4
|
1.0
|
CE1
|
A:HIS399
|
3.5
|
24.1
|
1.0
|
CU
|
A:CU499
|
3.6
|
38.0
|
1.0
|
CG
|
A:HIS66
|
3.6
|
23.4
|
1.0
|
CD2
|
A:HIS399
|
3.6
|
25.6
|
1.0
|
CE1
|
A:HIS66
|
3.7
|
23.5
|
1.0
|
CA
|
A:HIS66
|
3.8
|
24.1
|
1.0
|
ND1
|
A:HIS399
|
3.8
|
25.0
|
1.0
|
ND1
|
A:HIS397
|
3.9
|
30.0
|
1.0
|
CG
|
A:HIS397
|
3.9
|
26.8
|
1.0
|
CG
|
A:HIS399
|
3.9
|
26.5
|
1.0
|
CD2
|
A:HIS66
|
4.0
|
21.1
|
1.0
|
NE2
|
A:HIS66
|
4.0
|
21.1
|
1.0
|
ND1
|
A:HIS64
|
4.1
|
27.3
|
1.0
|
CB
|
A:HIS66
|
4.1
|
24.1
|
1.0
|
CG
|
A:HIS64
|
4.1
|
25.9
|
1.0
|
N
|
A:GLY67
|
4.2
|
25.4
|
1.0
|
C
|
A:HIS66
|
4.5
|
25.0
|
1.0
|
O
|
A:HOH1106
|
4.6
|
42.5
|
1.0
|
CA
|
A:HIS399
|
4.7
|
27.1
|
1.0
|
N
|
A:HIS66
|
4.8
|
24.7
|
1.0
|
O
|
A:HOH1017
|
4.8
|
26.2
|
1.0
|
CB
|
A:HIS399
|
4.9
|
27.2
|
1.0
|
NE2
|
A:HIS109
|
4.9
|
20.8
|
1.0
|
|
Copper binding site 3 out
of 4 in 2hrh
Go back to
Copper Binding Sites List in 2hrh
Copper binding site 3 out
of 4 in the Crystal Structure of Blue Laccase From Trametes Trogii
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 Blue Laccase From Trametes Trogii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu499
b:38.0
occ:1.00
|
NE2
|
A:HIS399
|
2.1
|
28.0
|
1.0
|
NE2
|
A:HIS449
|
2.2
|
31.3
|
1.0
|
NE2
|
A:HIS111
|
2.4
|
21.0
|
1.0
|
CE1
|
A:HIS399
|
3.0
|
24.1
|
1.0
|
CE1
|
A:HIS449
|
3.1
|
30.7
|
1.0
|
CD2
|
A:HIS111
|
3.2
|
19.9
|
1.0
|
CU
|
A:CU500
|
3.2
|
44.3
|
1.0
|
CD2
|
A:HIS397
|
3.2
|
28.4
|
1.0
|
CD2
|
A:HIS399
|
3.2
|
25.6
|
1.0
|
CD2
|
A:HIS449
|
3.2
|
29.6
|
1.0
|
CE1
|
A:HIS111
|
3.5
|
22.1
|
1.0
|
CU
|
A:CU498
|
3.6
|
59.5
|
1.0
|
NE2
|
A:HIS397
|
3.8
|
31.0
|
1.0
|
CD2
|
A:HIS64
|
4.1
|
25.0
|
1.0
|
ND1
|
A:HIS399
|
4.1
|
25.0
|
1.0
|
NE2
|
A:HIS64
|
4.2
|
29.8
|
1.0
|
ND1
|
A:HIS449
|
4.3
|
28.8
|
1.0
|
CG
|
A:HIS399
|
4.3
|
26.5
|
1.0
|
CG
|
A:HIS449
|
4.4
|
28.1
|
1.0
|
CE1
|
A:HIS109
|
4.4
|
21.1
|
1.0
|
CG
|
A:HIS397
|
4.4
|
26.8
|
1.0
|
CG
|
A:HIS111
|
4.4
|
22.6
|
1.0
|
NE2
|
A:HIS451
|
4.4
|
28.5
|
1.0
|
CD2
|
A:HIS451
|
4.5
|
25.0
|
1.0
|
ND1
|
A:HIS111
|
4.6
|
23.1
|
1.0
|
NE2
|
A:HIS109
|
4.8
|
20.8
|
1.0
|
CG
|
A:HIS64
|
4.8
|
25.9
|
1.0
|
ND1
|
A:HIS66
|
5.0
|
21.4
|
1.0
|
|
Copper binding site 4 out
of 4 in 2hrh
Go back to
Copper Binding Sites List in 2hrh
Copper binding site 4 out
of 4 in the Crystal Structure of Blue Laccase From Trametes Trogii
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 Blue Laccase From Trametes Trogii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu500
b:44.3
occ:1.00
|
ND1
|
A:HIS66
|
2.1
|
21.4
|
1.0
|
NE2
|
A:HIS109
|
2.3
|
20.8
|
1.0
|
NE2
|
A:HIS451
|
2.4
|
28.5
|
1.0
|
CE1
|
A:HIS66
|
2.7
|
23.5
|
1.0
|
CE1
|
A:HIS109
|
2.9
|
21.1
|
1.0
|
CD2
|
A:HIS451
|
3.1
|
25.0
|
1.0
|
CU
|
A:CU499
|
3.2
|
38.0
|
1.0
|
CU
|
A:CU498
|
3.3
|
59.5
|
1.0
|
CG
|
A:HIS66
|
3.3
|
23.4
|
1.0
|
CE1
|
A:HIS451
|
3.5
|
26.5
|
1.0
|
CD2
|
A:HIS64
|
3.6
|
25.0
|
1.0
|
CD2
|
A:HIS109
|
3.6
|
21.2
|
1.0
|
CD2
|
A:HIS397
|
3.7
|
28.4
|
1.0
|
NE2
|
A:HIS397
|
3.8
|
31.0
|
1.0
|
NE2
|
A:HIS66
|
3.9
|
21.1
|
1.0
|
CB
|
A:HIS66
|
4.0
|
24.1
|
1.0
|
NE2
|
A:HIS64
|
4.0
|
29.8
|
1.0
|
ND1
|
A:HIS109
|
4.1
|
18.9
|
1.0
|
CD2
|
A:HIS66
|
4.2
|
21.1
|
1.0
|
CG
|
A:HIS451
|
4.3
|
25.2
|
1.0
|
ND1
|
A:HIS451
|
4.5
|
25.9
|
1.0
|
CG
|
A:HIS109
|
4.5
|
21.1
|
1.0
|
CZ2
|
A:TRP107
|
4.5
|
20.3
|
1.0
|
CG
|
A:HIS397
|
4.6
|
26.8
|
1.0
|
NE2
|
A:HIS449
|
4.6
|
31.3
|
1.0
|
CD2
|
A:HIS111
|
4.7
|
19.9
|
1.0
|
CE1
|
A:HIS397
|
4.7
|
28.8
|
1.0
|
NE2
|
A:HIS399
|
4.7
|
28.0
|
1.0
|
CA
|
A:HIS66
|
4.8
|
24.1
|
1.0
|
NE2
|
A:HIS111
|
4.8
|
21.0
|
1.0
|
CE1
|
A:HIS449
|
4.8
|
30.7
|
1.0
|
CG
|
A:HIS64
|
4.8
|
25.9
|
1.0
|
CB
|
A:ALA240
|
4.9
|
23.1
|
1.0
|
CE2
|
A:TRP107
|
4.9
|
19.6
|
1.0
|
NE1
|
A:TRP107
|
4.9
|
21.5
|
1.0
|
|
Reference:
I.Matera,
A.Gullotto,
S.Tilli,
M.Ferraroni,
A.Scozzafava,
F.Briganti.
Crystal Structure of the Blue Multicopper Oxidase From the White-Rot Fungus Trametes Trogii Complexed with P-Toluate Inorg.Chim.Acta. V. 361 4129 2008.
ISSN: ISSN 0020-1693
DOI: 10.1016/J.ICA.2008.03.091
Page generated: Tue Jul 30 23:39:44 2024
|