Copper in PDB 2xyb: Crystal Structure of A Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus
Enzymatic activity of Crystal Structure of A Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus
All present enzymatic activity of Crystal Structure of A Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus:
1.10.3.2;
Protein crystallography data
The structure of Crystal Structure of A Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus, PDB code: 2xyb
was solved by
K.Piontek,
T.Choinowski,
M.Antorini,
I.Herpoel-Gimbert,
D.A.Plattner,
J.C.Sigoillot,
M.Asther,
K.Winterhalter,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
72.55 /
1.75
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
145.296,
62.902,
91.416,
90.00,
126.70,
90.00
|
R / Rfree (%)
|
16.4 /
20.8
|
Other elements in 2xyb:
The structure of Crystal Structure of A Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus also contains other interesting chemical elements:
Copper Binding Sites:
The binding sites of Copper atom in the Crystal Structure of A Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus
(pdb code 2xyb). 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 A Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus, PDB code: 2xyb:
Jump to Copper binding site number:
1;
2;
3;
4;
Copper binding site 1 out
of 4 in 2xyb
Go back to
Copper Binding Sites List in 2xyb
Copper binding site 1 out
of 4 in the Crystal Structure of A Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus
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 A Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu501
b:29.4
occ:1.00
|
ND1
|
A:HIS456
|
2.0
|
27.0
|
1.0
|
ND1
|
A:HIS395
|
2.1
|
27.4
|
1.0
|
SG
|
A:CYS451
|
2.3
|
25.3
|
1.0
|
CE1
|
A:HIS456
|
3.0
|
27.4
|
1.0
|
CE1
|
A:HIS395
|
3.0
|
33.0
|
1.0
|
CG
|
A:HIS456
|
3.0
|
25.2
|
1.0
|
CG
|
A:HIS395
|
3.1
|
28.6
|
1.0
|
CB
|
A:CYS451
|
3.3
|
20.0
|
1.0
|
CB
|
A:HIS456
|
3.4
|
27.1
|
1.0
|
CB
|
A:HIS395
|
3.5
|
24.1
|
1.0
|
CD1
|
A:ILE453
|
3.6
|
24.1
|
1.0
|
CD2
|
A:PHE461
|
3.7
|
22.9
|
1.0
|
CB
|
A:ILE453
|
3.8
|
22.0
|
1.0
|
CE2
|
A:PHE461
|
3.9
|
20.7
|
1.0
|
CA
|
A:HIS395
|
3.9
|
26.5
|
1.0
|
CG1
|
A:ILE453
|
4.0
|
21.6
|
1.0
|
NE2
|
A:HIS456
|
4.1
|
25.7
|
1.0
|
NE2
|
A:HIS395
|
4.1
|
27.8
|
1.0
|
CD2
|
A:HIS456
|
4.2
|
28.0
|
1.0
|
CD2
|
A:HIS395
|
4.2
|
29.1
|
1.0
|
CG2
|
A:ILE453
|
4.6
|
25.9
|
1.0
|
CD
|
A:PRO396
|
4.6
|
21.5
|
1.0
|
O
|
A:GLY392
|
4.6
|
31.4
|
1.0
|
CA
|
A:CYS451
|
4.7
|
19.2
|
1.0
|
N
|
A:ILE453
|
4.7
|
25.2
|
1.0
|
CA
|
A:ILE453
|
4.8
|
22.4
|
1.0
|
CA
|
A:HIS456
|
4.9
|
25.2
|
1.0
|
C
|
A:HIS395
|
4.9
|
28.3
|
1.0
|
CG
|
A:PHE461
|
5.0
|
25.4
|
1.0
|
|
Copper binding site 2 out
of 4 in 2xyb
Go back to
Copper Binding Sites List in 2xyb
Copper binding site 2 out
of 4 in the Crystal Structure of A Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus
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 A Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu502
b:29.7
occ:1.00
|
O2
|
A:PER505
|
1.8
|
27.5
|
1.0
|
NE2
|
A:HIS400
|
2.0
|
24.1
|
1.0
|
NE2
|
A:HIS111
|
2.1
|
28.8
|
1.0
|
NE2
|
A:HIS450
|
2.1
|
25.1
|
1.0
|
CE1
|
A:HIS400
|
2.7
|
25.9
|
1.0
|
O1
|
A:PER505
|
3.0
|
30.0
|
1.0
|
CE1
|
A:HIS111
|
3.0
|
24.1
|
1.0
|
CD2
|
A:HIS111
|
3.1
|
25.8
|
1.0
|
CD2
|
A:HIS450
|
3.1
|
23.8
|
1.0
|
CE1
|
A:HIS450
|
3.1
|
28.4
|
1.0
|
CD2
|
A:HIS400
|
3.2
|
25.3
|
1.0
|
CD2
|
A:HIS398
|
3.6
|
23.2
|
1.0
|
O
|
A:HOH935
|
3.9
|
32.7
|
1.0
|
ND1
|
A:HIS400
|
4.0
|
24.2
|
1.0
|
ND1
|
A:HIS111
|
4.1
|
24.2
|
1.0
|
CU
|
A:CU504
|
4.1
|
36.0
|
1.0
|
ND1
|
A:HIS450
|
4.2
|
21.0
|
1.0
|
CG
|
A:HIS111
|
4.2
|
23.9
|
1.0
|
CG
|
A:HIS400
|
4.2
|
26.3
|
1.0
|
CG
|
A:HIS450
|
4.2
|
25.1
|
1.0
|
NE2
|
A:HIS398
|
4.3
|
23.4
|
1.0
|
CD2
|
A:PHE448
|
4.3
|
25.0
|
1.0
|
CD2
|
A:HIS64
|
4.4
|
22.9
|
1.0
|
NE2
|
A:HIS64
|
4.6
|
23.3
|
1.0
|
CB
|
A:PHE448
|
4.6
|
26.5
|
1.0
|
CG
|
A:PRO79
|
4.7
|
21.7
|
1.0
|
NE2
|
A:HIS452
|
4.7
|
25.9
|
1.0
|
CU
|
A:CU503
|
4.7
|
25.3
|
1.0
|
CG
|
A:HIS398
|
4.7
|
27.3
|
1.0
|
CD2
|
A:HIS452
|
4.8
|
22.7
|
1.0
|
CE1
|
A:HIS109
|
4.9
|
21.0
|
1.0
|
CG
|
A:PHE448
|
5.0
|
26.9
|
1.0
|
|
Copper binding site 3 out
of 4 in 2xyb
Go back to
Copper Binding Sites List in 2xyb
Copper binding site 3 out
of 4 in the Crystal Structure of A Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus
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 A Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu503
b:25.3
occ:1.00
|
O1
|
A:PER505
|
1.8
|
30.0
|
1.0
|
ND1
|
A:HIS66
|
2.0
|
22.4
|
1.0
|
NE2
|
A:HIS109
|
2.0
|
19.4
|
1.0
|
NE2
|
A:HIS452
|
2.1
|
25.9
|
1.0
|
CE1
|
A:HIS66
|
2.9
|
21.6
|
1.0
|
CE1
|
A:HIS452
|
2.9
|
25.0
|
1.0
|
CE1
|
A:HIS109
|
3.0
|
21.0
|
1.0
|
O2
|
A:PER505
|
3.0
|
27.5
|
1.0
|
CD2
|
A:HIS109
|
3.1
|
19.4
|
1.0
|
CG
|
A:HIS66
|
3.1
|
22.1
|
1.0
|
CD2
|
A:HIS452
|
3.2
|
22.7
|
1.0
|
CB
|
A:HIS66
|
3.5
|
19.1
|
1.0
|
CZ2
|
A:TRP107
|
3.8
|
18.8
|
1.0
|
CD2
|
A:HIS64
|
3.9
|
22.9
|
1.0
|
CU
|
A:CU504
|
4.0
|
36.0
|
1.0
|
CE2
|
A:TRP107
|
4.1
|
21.0
|
1.0
|
NE2
|
A:HIS66
|
4.1
|
20.3
|
1.0
|
ND1
|
A:HIS109
|
4.1
|
18.5
|
1.0
|
ND1
|
A:HIS452
|
4.1
|
21.1
|
1.0
|
NE1
|
A:TRP107
|
4.2
|
21.7
|
1.0
|
CD2
|
A:HIS66
|
4.2
|
22.5
|
1.0
|
CG
|
A:HIS109
|
4.2
|
18.5
|
1.0
|
CD2
|
A:HIS398
|
4.3
|
23.2
|
1.0
|
CG
|
A:HIS452
|
4.3
|
25.5
|
1.0
|
CB
|
A:ALA241
|
4.3
|
19.1
|
1.0
|
O
|
A:HOH935
|
4.4
|
32.7
|
1.0
|
NE2
|
A:HIS64
|
4.4
|
23.3
|
1.0
|
NE2
|
A:HIS398
|
4.5
|
23.4
|
1.0
|
CH2
|
A:TRP107
|
4.5
|
21.8
|
1.0
|
CA
|
A:HIS66
|
4.6
|
22.1
|
1.0
|
CU
|
A:CU502
|
4.7
|
29.7
|
1.0
|
CD2
|
A:TRP107
|
5.0
|
19.2
|
1.0
|
|
Copper binding site 4 out
of 4 in 2xyb
Go back to
Copper Binding Sites List in 2xyb
Copper binding site 4 out
of 4 in the Crystal Structure of A Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus
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 A Fully Functional Laccase From the Ligninolytic Fungus Pycnoporus Cinnabarinus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu504
b:36.0
occ:1.00
|
NE2
|
A:HIS398
|
2.0
|
23.4
|
1.0
|
NE2
|
A:HIS64
|
2.0
|
23.3
|
1.0
|
O
|
A:HOH874
|
2.8
|
26.6
|
1.0
|
CD2
|
A:HIS398
|
2.9
|
23.2
|
1.0
|
CE1
|
A:HIS398
|
2.9
|
25.2
|
1.0
|
CD2
|
A:HIS64
|
2.9
|
22.9
|
1.0
|
CE1
|
A:HIS64
|
3.0
|
24.5
|
1.0
|
O1
|
A:PER505
|
3.1
|
30.0
|
1.0
|
ND1
|
A:HIS66
|
3.4
|
22.4
|
1.0
|
NE2
|
A:HIS400
|
3.4
|
24.1
|
1.0
|
CE1
|
A:HIS400
|
3.5
|
25.9
|
1.0
|
CD2
|
A:HIS400
|
3.6
|
25.3
|
1.0
|
CG
|
A:HIS66
|
3.7
|
22.1
|
1.0
|
CE1
|
A:HIS66
|
3.7
|
21.6
|
1.0
|
ND1
|
A:HIS400
|
3.8
|
24.2
|
1.0
|
O2
|
A:PER505
|
3.8
|
27.5
|
1.0
|
CA
|
A:HIS66
|
3.9
|
22.1
|
1.0
|
CG
|
A:HIS400
|
3.9
|
26.3
|
1.0
|
CU
|
A:CU503
|
4.0
|
25.3
|
1.0
|
CG
|
A:HIS398
|
4.0
|
27.3
|
1.0
|
ND1
|
A:HIS64
|
4.0
|
20.5
|
1.0
|
ND1
|
A:HIS398
|
4.0
|
27.1
|
1.0
|
CG
|
A:HIS64
|
4.0
|
20.8
|
1.0
|
CD2
|
A:HIS66
|
4.1
|
22.5
|
1.0
|
CB
|
A:HIS66
|
4.1
|
19.1
|
1.0
|
CU
|
A:CU502
|
4.1
|
29.7
|
1.0
|
N
|
A:GLY67
|
4.2
|
17.8
|
1.0
|
NE2
|
A:HIS66
|
4.2
|
20.3
|
1.0
|
C
|
A:HIS66
|
4.6
|
17.6
|
1.0
|
O
|
A:HOH748
|
4.6
|
27.6
|
1.0
|
CA
|
A:HIS400
|
4.7
|
22.7
|
1.0
|
CB
|
A:HIS400
|
4.8
|
20.1
|
1.0
|
O
|
A:HOH993
|
4.8
|
32.3
|
1.0
|
N
|
A:HIS66
|
4.9
|
20.6
|
1.0
|
O
|
A:TRP65
|
5.0
|
20.3
|
1.0
|
|
Reference:
K.Piontek,
T.Choinowski,
M.Antorini,
I.Herpoel-Gimbert,
M.Asther,
D.A.Plattner.
Substrate Binding and Copper Geometry in Laccases To Be Published.
Page generated: Wed Jul 31 00:17:32 2024
|