Copper in PDB 1a65: Type-2 Cu-Depleted Laccase From Coprinus Cinereus
Enzymatic activity of Type-2 Cu-Depleted Laccase From Coprinus Cinereus
All present enzymatic activity of Type-2 Cu-Depleted Laccase From Coprinus Cinereus:
1.10.3.2;
Protein crystallography data
The structure of Type-2 Cu-Depleted Laccase From Coprinus Cinereus, PDB code: 1a65
was solved by
V.Ducros,
W.Brzozowski,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
12.00 /
2.23
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
45.390,
85.720,
143.070,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
16 /
22
|
Copper Binding Sites:
The binding sites of Copper atom in the Type-2 Cu-Depleted Laccase From Coprinus Cinereus
(pdb code 1a65). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the
Type-2 Cu-Depleted Laccase From Coprinus Cinereus, PDB code: 1a65:
Jump to Copper binding site number:
1;
2;
3;
Copper binding site 1 out
of 3 in 1a65
Go back to
Copper Binding Sites List in 1a65
Copper binding site 1 out
of 3 in the Type-2 Cu-Depleted Laccase From Coprinus Cinereus
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Type-2 Cu-Depleted Laccase From Coprinus Cinereus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu901
b:29.5
occ:1.00
|
ND1
|
A:HIS457
|
1.9
|
21.4
|
1.0
|
ND1
|
A:HIS396
|
1.9
|
16.2
|
1.0
|
SG
|
A:CYS452
|
2.3
|
19.8
|
1.0
|
CE1
|
A:HIS457
|
2.8
|
22.5
|
1.0
|
CE1
|
A:HIS396
|
2.8
|
18.2
|
1.0
|
CG
|
A:HIS457
|
2.9
|
22.5
|
1.0
|
CG
|
A:HIS396
|
3.0
|
18.2
|
1.0
|
CB
|
A:CYS452
|
3.3
|
18.2
|
1.0
|
CB
|
A:HIS457
|
3.4
|
21.0
|
1.0
|
CB
|
A:HIS396
|
3.5
|
15.4
|
1.0
|
CD2
|
A:LEU462
|
3.5
|
21.0
|
1.0
|
CD1
|
A:ILE454
|
3.8
|
16.3
|
1.0
|
CA
|
A:HIS396
|
3.9
|
15.1
|
1.0
|
NE2
|
A:HIS457
|
3.9
|
23.2
|
1.0
|
NE2
|
A:HIS396
|
4.0
|
19.1
|
1.0
|
CD2
|
A:HIS457
|
4.0
|
22.5
|
1.0
|
CB
|
A:ILE454
|
4.0
|
16.5
|
1.0
|
CD2
|
A:HIS396
|
4.1
|
17.0
|
1.0
|
CD
|
A:PRO397
|
4.4
|
14.4
|
1.0
|
CG1
|
A:ILE454
|
4.4
|
15.3
|
1.0
|
O
|
A:GLY393
|
4.7
|
26.7
|
1.0
|
CA
|
A:CYS452
|
4.7
|
16.3
|
1.0
|
CG2
|
A:ILE454
|
4.7
|
14.2
|
1.0
|
CG
|
A:LEU462
|
4.8
|
20.4
|
1.0
|
CA
|
A:HIS457
|
4.9
|
22.6
|
1.0
|
N
|
A:HIS396
|
4.9
|
17.0
|
1.0
|
C
|
A:HIS396
|
4.9
|
15.4
|
1.0
|
N
|
A:ILE454
|
4.9
|
15.3
|
1.0
|
N
|
A:PRO397
|
5.0
|
14.7
|
1.0
|
|
Copper binding site 2 out
of 3 in 1a65
Go back to
Copper Binding Sites List in 1a65
Copper binding site 2 out
of 3 in the Type-2 Cu-Depleted Laccase From Coprinus Cinereus
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Type-2 Cu-Depleted Laccase From Coprinus Cinereus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu902
b:27.0
occ:1.00
|
NE2
|
A:HIS401
|
2.1
|
12.4
|
1.0
|
NE2
|
A:HIS111
|
2.1
|
15.3
|
1.0
|
NE2
|
A:HIS399
|
2.1
|
17.5
|
1.0
|
O
|
A:O904
|
2.1
|
27.0
|
1.0
|
NE2
|
A:HIS451
|
2.1
|
19.0
|
1.0
|
CE1
|
A:HIS111
|
2.9
|
16.3
|
1.0
|
CE1
|
A:HIS451
|
2.9
|
17.8
|
1.0
|
CE1
|
A:HIS401
|
2.9
|
12.6
|
1.0
|
CD2
|
A:HIS399
|
3.0
|
17.6
|
1.0
|
CD2
|
A:HIS401
|
3.1
|
12.3
|
1.0
|
CE1
|
A:HIS399
|
3.2
|
15.6
|
1.0
|
CD2
|
A:HIS111
|
3.3
|
14.7
|
1.0
|
CD2
|
A:HIS451
|
3.3
|
17.9
|
1.0
|
O
|
A:HOH1029
|
4.0
|
28.3
|
1.0
|
ND1
|
A:HIS401
|
4.1
|
15.0
|
1.0
|
ND1
|
A:HIS451
|
4.1
|
18.1
|
1.0
|
ND1
|
A:HIS111
|
4.1
|
14.6
|
1.0
|
CG
|
A:HIS399
|
4.2
|
16.3
|
1.0
|
CG
|
A:HIS401
|
4.2
|
14.5
|
1.0
|
ND1
|
A:HIS399
|
4.2
|
15.3
|
1.0
|
CG
|
A:HIS111
|
4.3
|
15.3
|
1.0
|
CD2
|
A:HIS64
|
4.3
|
14.8
|
1.0
|
CG
|
A:HIS451
|
4.3
|
17.0
|
1.0
|
NE2
|
A:HIS64
|
4.4
|
13.6
|
1.0
|
CD2
|
A:PHE449
|
4.7
|
20.7
|
1.0
|
CD2
|
A:HIS453
|
4.7
|
12.7
|
1.0
|
NE2
|
A:HIS453
|
4.7
|
13.2
|
1.0
|
CB
|
A:PHE449
|
4.8
|
16.2
|
1.0
|
CU
|
A:CU903
|
4.9
|
21.4
|
1.0
|
CG
|
A:HIS64
|
5.0
|
14.5
|
1.0
|
|
Copper binding site 3 out
of 3 in 1a65
Go back to
Copper Binding Sites List in 1a65
Copper binding site 3 out
of 3 in the Type-2 Cu-Depleted Laccase From Coprinus Cinereus
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Type-2 Cu-Depleted Laccase From Coprinus Cinereus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu903
b:21.4
occ:1.00
|
NE2
|
A:HIS109
|
2.0
|
7.9
|
1.0
|
ND1
|
A:HIS66
|
2.1
|
13.1
|
1.0
|
NE2
|
A:HIS453
|
2.3
|
13.2
|
1.0
|
CD2
|
A:HIS109
|
2.9
|
10.8
|
1.0
|
CE1
|
A:HIS109
|
3.0
|
8.5
|
1.0
|
CE1
|
A:HIS66
|
3.0
|
12.5
|
1.0
|
CG
|
A:HIS66
|
3.0
|
11.3
|
1.0
|
CE1
|
A:HIS453
|
3.1
|
12.4
|
1.0
|
O
|
A:O904
|
3.1
|
27.0
|
1.0
|
CD2
|
A:HIS453
|
3.4
|
12.7
|
1.0
|
CB
|
A:HIS66
|
3.4
|
10.8
|
1.0
|
CZ2
|
A:TRP107
|
3.4
|
10.0
|
1.0
|
CD2
|
A:HIS64
|
3.7
|
14.8
|
1.0
|
CE2
|
A:TRP107
|
3.8
|
9.9
|
1.0
|
NE1
|
A:TRP107
|
4.0
|
10.6
|
1.0
|
CE1
|
A:HIS399
|
4.1
|
15.6
|
1.0
|
ND1
|
A:HIS109
|
4.1
|
9.9
|
1.0
|
CG
|
A:HIS109
|
4.1
|
12.3
|
1.0
|
NE2
|
A:HIS66
|
4.1
|
13.7
|
1.0
|
CD2
|
A:HIS66
|
4.1
|
13.5
|
1.0
|
CH2
|
A:TRP107
|
4.2
|
10.1
|
1.0
|
NE2
|
A:HIS399
|
4.3
|
17.5
|
1.0
|
ND1
|
A:HIS453
|
4.3
|
10.7
|
1.0
|
NE2
|
A:HIS64
|
4.3
|
13.6
|
1.0
|
CG
|
A:HIS453
|
4.4
|
11.9
|
1.0
|
CA
|
A:HIS66
|
4.6
|
12.0
|
1.0
|
ND1
|
A:HIS399
|
4.6
|
15.3
|
1.0
|
CD2
|
A:TRP107
|
4.8
|
9.2
|
1.0
|
CG
|
A:HIS64
|
4.9
|
14.5
|
1.0
|
CD2
|
A:HIS399
|
4.9
|
17.6
|
1.0
|
CU
|
A:CU902
|
4.9
|
27.0
|
1.0
|
CD1
|
A:TRP107
|
5.0
|
10.5
|
1.0
|
|
Reference:
V.Ducros,
A.M.Brzozowski,
K.S.Wilson,
S.H.Brown,
P.Ostergaard,
P.Schneider,
D.S.Yaver,
A.H.Pedersen,
G.J.Davies.
Crystal Structure of the Type-2 Cu Depleted Laccase From Coprinus Cinereus at 2.2 A Resolution. Nat.Struct.Biol. V. 5 310 1998.
ISSN: ISSN 1072-8368
PubMed: 9546223
DOI: 10.1038/NSB0498-310
Page generated: Tue Jul 30 21:27:41 2024
|