Copper in PDB 2yxv: The Deletion Mutant of Multicopper Oxidase Cueo
Protein crystallography data
The structure of The Deletion Mutant of Multicopper Oxidase Cueo, PDB code: 2yxv
was solved by
Y.Higuchi,
H.Komori,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
24.40 /
1.81
|
|
Space group
|
P 1
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
49.982,
50.947,
86.050,
83.20,
90.83,
66.66
|
|
R / Rfree (%)
|
17.1 /
20.8
|
Copper Binding Sites:
The binding sites of Copper atom in the The Deletion Mutant of Multicopper Oxidase Cueo
(pdb code 2yxv). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 8 binding sites of Copper where determined in the
The Deletion Mutant of Multicopper Oxidase Cueo, PDB code: 2yxv:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Copper binding site 1 out
of 8 in 2yxv
Go back to
Copper Binding Sites List in 2yxv
Copper binding site 1 out
of 8 in the The Deletion Mutant of Multicopper Oxidase Cueo
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of The Deletion Mutant of Multicopper Oxidase Cueo within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu701
b:26.5
occ:1.00
|
ND1
|
A:HIS505
|
2.0
|
24.7
|
1.0
|
|
ND1
|
A:HIS443
|
2.0
|
22.8
|
1.0
|
|
SG
|
A:CYS500
|
2.1
|
23.5
|
1.0
|
|
CE1
|
A:HIS505
|
3.0
|
24.3
|
1.0
|
|
CG
|
A:HIS505
|
3.0
|
24.4
|
1.0
|
|
CE1
|
A:HIS443
|
3.0
|
24.3
|
1.0
|
|
CG
|
A:HIS443
|
3.1
|
23.9
|
1.0
|
|
CB
|
A:CYS500
|
3.2
|
22.9
|
1.0
|
|
SD
|
A:MET510
|
3.3
|
25.1
|
1.0
|
|
CB
|
A:HIS505
|
3.3
|
23.8
|
1.0
|
|
CB
|
A:HIS443
|
3.4
|
23.8
|
1.0
|
|
CA
|
A:HIS443
|
3.7
|
24.8
|
1.0
|
|
O
|
A:LEU442
|
3.8
|
26.2
|
1.0
|
|
CE
|
A:MET510
|
3.9
|
25.4
|
1.0
|
|
CB
|
A:LEU502
|
4.0
|
23.6
|
1.0
|
|
NE2
|
A:HIS505
|
4.1
|
24.0
|
1.0
|
|
CD2
|
A:HIS505
|
4.1
|
24.7
|
1.0
|
|
NE2
|
A:HIS443
|
4.1
|
22.5
|
1.0
|
|
CD2
|
A:HIS443
|
4.2
|
22.5
|
1.0
|
|
C
|
A:LEU442
|
4.4
|
26.0
|
1.0
|
|
N
|
A:HIS443
|
4.5
|
24.6
|
1.0
|
|
CA
|
A:CYS500
|
4.6
|
22.9
|
1.0
|
|
CD1
|
A:LEU502
|
4.6
|
24.5
|
1.0
|
|
CG
|
A:LEU502
|
4.8
|
24.5
|
1.0
|
|
CG
|
A:MET510
|
4.8
|
22.8
|
1.0
|
|
CA
|
A:HIS505
|
4.9
|
24.1
|
1.0
|
|
O
|
A:LEU502
|
4.9
|
22.8
|
1.0
|
|
C
|
A:HIS443
|
4.9
|
24.1
|
1.0
|
|
N
|
A:LEU502
|
4.9
|
23.8
|
1.0
|
|
Copper binding site 2 out
of 8 in 2yxv
Go back to
Copper Binding Sites List in 2yxv
Copper binding site 2 out
of 8 in the The Deletion Mutant of Multicopper Oxidase Cueo
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of The Deletion Mutant of Multicopper Oxidase Cueo within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu703
b:38.0
occ:1.00
|
NE2
|
A:HIS446
|
2.0
|
27.3
|
1.0
|
|
NE2
|
A:HIS101
|
2.0
|
25.7
|
1.0
|
|
O
|
A:HOH745
|
2.5
|
21.1
|
1.0
|
|
O1
|
A:C2O702
|
2.7
|
31.0
|
1.0
|
|
CD2
|
A:HIS446
|
2.9
|
25.1
|
1.0
|
|
CE1
|
A:HIS101
|
2.9
|
25.1
|
1.0
|
|
CE1
|
A:HIS446
|
3.0
|
25.3
|
1.0
|
|
CD2
|
A:HIS101
|
3.0
|
25.6
|
1.0
|
|
CD2
|
A:HIS448
|
3.0
|
25.3
|
1.0
|
|
NE2
|
A:HIS448
|
3.1
|
26.7
|
1.0
|
|
CU2
|
A:C2O702
|
3.5
|
33.5
|
1.0
|
|
CA
|
A:HIS103
|
3.5
|
23.6
|
1.0
|
|
CG
|
A:HIS103
|
3.5
|
23.8
|
1.0
|
|
ND1
|
A:HIS103
|
3.7
|
25.6
|
1.0
|
|
CB
|
A:HIS103
|
3.7
|
23.8
|
1.0
|
|
CG
|
A:HIS448
|
3.7
|
25.3
|
1.0
|
|
CE1
|
A:HIS448
|
3.8
|
24.9
|
1.0
|
|
CU3
|
A:C2O702
|
3.9
|
29.4
|
1.0
|
|
ND1
|
A:HIS101
|
4.0
|
24.3
|
1.0
|
|
CG
|
A:HIS446
|
4.0
|
23.5
|
1.0
|
|
ND1
|
A:HIS446
|
4.1
|
24.6
|
1.0
|
|
CD2
|
A:HIS103
|
4.1
|
23.8
|
1.0
|
|
ND1
|
A:HIS448
|
4.1
|
25.3
|
1.0
|
|
CG
|
A:HIS101
|
4.1
|
24.7
|
1.0
|
|
N
|
A:GLY104
|
4.2
|
23.8
|
1.0
|
|
CE1
|
A:HIS103
|
4.2
|
23.7
|
1.0
|
|
C
|
A:HIS103
|
4.4
|
23.7
|
1.0
|
|
N
|
A:HIS103
|
4.4
|
23.4
|
1.0
|
|
NE2
|
A:HIS103
|
4.5
|
23.4
|
1.0
|
|
O
|
A:HOH732
|
4.5
|
24.3
|
1.0
|
|
CA
|
A:HIS448
|
4.5
|
24.2
|
1.0
|
|
CB
|
A:HIS448
|
4.6
|
25.0
|
1.0
|
|
O
|
A:TRP102
|
4.7
|
23.2
|
1.0
|
|
O
|
A:HOH720
|
4.7
|
16.0
|
1.0
|
|
C
|
A:TRP102
|
4.9
|
23.5
|
1.0
|
|
NE2
|
A:HIS499
|
5.0
|
25.4
|
1.0
|
|
N
|
A:HIS448
|
5.0
|
23.8
|
1.0
|
|
Copper binding site 3 out
of 8 in 2yxv
Go back to
Copper Binding Sites List in 2yxv
Copper binding site 3 out
of 8 in the The Deletion Mutant of Multicopper Oxidase Cueo
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of The Deletion Mutant of Multicopper Oxidase Cueo within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu702
b:33.5
occ:1.00
|
CU2
|
A:C2O702
|
0.0
|
33.5
|
1.0
|
|
O1
|
A:C2O702
|
2.0
|
31.0
|
1.0
|
|
NE2
|
A:HIS143
|
2.0
|
29.2
|
1.0
|
|
NE2
|
A:HIS448
|
2.0
|
26.7
|
1.0
|
|
NE2
|
A:HIS499
|
2.0
|
25.4
|
1.0
|
|
CE1
|
A:HIS499
|
2.9
|
23.4
|
1.0
|
|
CE1
|
A:HIS448
|
2.9
|
24.9
|
1.0
|
|
CD2
|
A:HIS143
|
3.0
|
28.0
|
1.0
|
|
CE1
|
A:HIS143
|
3.1
|
28.0
|
1.0
|
|
CD2
|
A:HIS448
|
3.1
|
25.3
|
1.0
|
|
CD2
|
A:HIS499
|
3.2
|
25.1
|
1.0
|
|
CD2
|
A:HIS446
|
3.5
|
25.1
|
1.0
|
|
CU
|
A:CU703
|
3.5
|
38.0
|
1.0
|
|
CU3
|
A:C2O702
|
3.8
|
29.4
|
1.0
|
|
NE2
|
A:HIS101
|
3.8
|
25.7
|
1.0
|
|
CD2
|
A:HIS101
|
3.9
|
25.6
|
1.0
|
|
NE2
|
A:HIS446
|
4.0
|
27.3
|
1.0
|
|
ND1
|
A:HIS499
|
4.0
|
24.0
|
1.0
|
|
ND1
|
A:HIS448
|
4.1
|
25.3
|
1.0
|
|
CG
|
A:HIS143
|
4.1
|
26.5
|
1.0
|
|
ND1
|
A:HIS143
|
4.1
|
26.3
|
1.0
|
|
CG
|
A:HIS448
|
4.2
|
25.3
|
1.0
|
|
CG
|
A:HIS499
|
4.2
|
22.6
|
1.0
|
|
CE1
|
A:HIS141
|
4.5
|
22.8
|
1.0
|
|
CD2
|
A:HIS501
|
4.5
|
25.0
|
1.0
|
|
NE2
|
A:HIS501
|
4.6
|
24.5
|
1.0
|
|
CE1
|
A:HIS101
|
4.6
|
25.1
|
1.0
|
|
CG
|
A:HIS446
|
4.7
|
23.5
|
1.0
|
|
CG
|
A:HIS101
|
4.7
|
24.7
|
1.0
|
|
NE2
|
A:HIS141
|
4.8
|
23.5
|
1.0
|
|
OE1
|
A:GLU506
|
4.9
|
32.5
|
1.0
|
|
CB
|
A:MET497
|
4.9
|
24.0
|
1.0
|
|
Copper binding site 4 out
of 8 in 2yxv
Go back to
Copper Binding Sites List in 2yxv
Copper binding site 4 out
of 8 in the The Deletion Mutant of Multicopper Oxidase Cueo
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of The Deletion Mutant of Multicopper Oxidase Cueo within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu702
b:29.4
occ:1.00
|
CU3
|
A:C2O702
|
0.0
|
29.4
|
1.0
|
|
O1
|
A:C2O702
|
2.0
|
31.0
|
1.0
|
|
NE2
|
A:HIS501
|
2.0
|
24.5
|
1.0
|
|
NE2
|
A:HIS141
|
2.1
|
23.5
|
1.0
|
|
ND1
|
A:HIS103
|
2.1
|
25.6
|
1.0
|
|
CE1
|
A:HIS141
|
2.9
|
22.8
|
1.0
|
|
CD2
|
A:HIS501
|
3.0
|
25.0
|
1.0
|
|
CE1
|
A:HIS501
|
3.0
|
25.1
|
1.0
|
|
CE1
|
A:HIS103
|
3.1
|
23.7
|
1.0
|
|
CG
|
A:HIS103
|
3.2
|
23.8
|
1.0
|
|
CD2
|
A:HIS141
|
3.2
|
23.1
|
1.0
|
|
CB
|
A:HIS103
|
3.5
|
23.8
|
1.0
|
|
CU2
|
A:C2O702
|
3.8
|
33.5
|
1.0
|
|
CU
|
A:CU703
|
3.9
|
38.0
|
1.0
|
|
CZ2
|
A:TRP139
|
4.1
|
24.1
|
1.0
|
|
CD2
|
A:HIS446
|
4.1
|
25.1
|
1.0
|
|
ND1
|
A:HIS141
|
4.1
|
23.1
|
1.0
|
|
CD2
|
A:HIS101
|
4.1
|
25.6
|
1.0
|
|
CG
|
A:HIS501
|
4.1
|
23.8
|
1.0
|
|
ND1
|
A:HIS501
|
4.1
|
24.9
|
1.0
|
|
NE2
|
A:HIS103
|
4.2
|
23.4
|
1.0
|
|
NE2
|
A:HIS446
|
4.2
|
27.3
|
1.0
|
|
CD2
|
A:HIS103
|
4.3
|
23.8
|
1.0
|
|
CG
|
A:HIS141
|
4.3
|
23.4
|
1.0
|
|
CE2
|
A:TRP139
|
4.4
|
24.2
|
1.0
|
|
NE2
|
A:HIS101
|
4.4
|
25.7
|
1.0
|
|
NE1
|
A:TRP139
|
4.5
|
24.4
|
1.0
|
|
CA
|
A:HIS103
|
4.7
|
23.6
|
1.0
|
|
CE1
|
A:HIS499
|
4.8
|
23.4
|
1.0
|
|
CH2
|
A:TRP139
|
4.8
|
23.6
|
1.0
|
|
NE2
|
A:HIS143
|
4.9
|
29.2
|
1.0
|
|
CG
|
A:HIS446
|
4.9
|
23.5
|
1.0
|
|
NE2
|
A:HIS499
|
4.9
|
25.4
|
1.0
|
|
CD2
|
A:HIS143
|
5.0
|
28.0
|
1.0
|
|
Copper binding site 5 out
of 8 in 2yxv
Go back to
Copper Binding Sites List in 2yxv
Copper binding site 5 out
of 8 in the The Deletion Mutant of Multicopper Oxidase Cueo
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 5 of The Deletion Mutant of Multicopper Oxidase Cueo within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu701
b:26.0
occ:1.00
|
ND1
|
B:HIS505
|
2.0
|
25.2
|
1.0
|
|
ND1
|
B:HIS443
|
2.0
|
22.1
|
1.0
|
|
SG
|
B:CYS500
|
2.2
|
24.9
|
1.0
|
|
CE1
|
B:HIS443
|
3.0
|
24.1
|
1.0
|
|
CG
|
B:HIS505
|
3.0
|
24.1
|
1.0
|
|
CE1
|
B:HIS505
|
3.0
|
26.1
|
1.0
|
|
CG
|
B:HIS443
|
3.0
|
24.0
|
1.0
|
|
CB
|
B:CYS500
|
3.2
|
23.5
|
1.0
|
|
CB
|
B:HIS505
|
3.3
|
24.4
|
1.0
|
|
SD
|
B:MET510
|
3.4
|
24.4
|
1.0
|
|
CB
|
B:HIS443
|
3.4
|
24.8
|
1.0
|
|
CA
|
B:HIS443
|
3.7
|
25.0
|
1.0
|
|
O
|
B:LEU442
|
3.9
|
26.3
|
1.0
|
|
CB
|
B:LEU502
|
4.0
|
23.2
|
1.0
|
|
NE2
|
B:HIS443
|
4.1
|
22.9
|
1.0
|
|
CE
|
B:MET510
|
4.1
|
24.7
|
1.0
|
|
NE2
|
B:HIS505
|
4.1
|
25.3
|
1.0
|
|
CD2
|
B:HIS505
|
4.1
|
25.2
|
1.0
|
|
CD2
|
B:HIS443
|
4.1
|
24.5
|
1.0
|
|
N
|
B:HIS443
|
4.4
|
25.4
|
1.0
|
|
C
|
B:LEU442
|
4.5
|
26.4
|
1.0
|
|
CA
|
B:CYS500
|
4.6
|
23.3
|
1.0
|
|
CD1
|
B:LEU502
|
4.6
|
23.8
|
1.0
|
|
CG
|
B:LEU502
|
4.8
|
23.4
|
1.0
|
|
CA
|
B:HIS505
|
4.8
|
24.2
|
1.0
|
|
CG
|
B:MET510
|
4.9
|
23.7
|
1.0
|
|
O
|
B:LEU502
|
4.9
|
23.2
|
1.0
|
|
C
|
B:HIS443
|
4.9
|
24.8
|
1.0
|
|
N
|
B:LEU502
|
5.0
|
23.3
|
1.0
|
|
Copper binding site 6 out
of 8 in 2yxv
Go back to
Copper Binding Sites List in 2yxv
Copper binding site 6 out
of 8 in the The Deletion Mutant of Multicopper Oxidase Cueo
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 6 of The Deletion Mutant of Multicopper Oxidase Cueo within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu703
b:38.4
occ:1.00
|
NE2
|
B:HIS446
|
1.9
|
26.1
|
1.0
|
|
NE2
|
B:HIS101
|
2.0
|
28.9
|
1.0
|
|
O
|
B:HOH748
|
2.5
|
20.2
|
1.0
|
|
O1
|
B:C2O702
|
2.6
|
32.8
|
1.0
|
|
CE1
|
B:HIS101
|
2.8
|
27.5
|
1.0
|
|
CD2
|
B:HIS446
|
2.9
|
24.5
|
1.0
|
|
CE1
|
B:HIS446
|
3.0
|
25.0
|
1.0
|
|
CD2
|
B:HIS448
|
3.0
|
24.2
|
1.0
|
|
NE2
|
B:HIS448
|
3.0
|
26.6
|
1.0
|
|
CD2
|
B:HIS101
|
3.1
|
27.9
|
1.0
|
|
CU2
|
B:C2O702
|
3.5
|
33.0
|
1.0
|
|
CA
|
B:HIS103
|
3.6
|
24.0
|
1.0
|
|
ND1
|
B:HIS103
|
3.6
|
26.3
|
1.0
|
|
CG
|
B:HIS448
|
3.6
|
24.2
|
1.0
|
|
CG
|
B:HIS103
|
3.6
|
24.9
|
1.0
|
|
CE1
|
B:HIS448
|
3.6
|
26.1
|
1.0
|
|
CB
|
B:HIS103
|
3.8
|
24.2
|
1.0
|
|
CU3
|
B:C2O702
|
3.9
|
29.5
|
1.0
|
|
ND1
|
B:HIS448
|
4.0
|
25.0
|
1.0
|
|
ND1
|
B:HIS101
|
4.0
|
26.2
|
1.0
|
|
CG
|
B:HIS446
|
4.0
|
24.4
|
1.0
|
|
ND1
|
B:HIS446
|
4.1
|
25.7
|
1.0
|
|
CG
|
B:HIS101
|
4.1
|
24.8
|
1.0
|
|
CE1
|
B:HIS103
|
4.1
|
23.3
|
1.0
|
|
CD2
|
B:HIS103
|
4.2
|
25.5
|
1.0
|
|
N
|
B:GLY104
|
4.3
|
24.6
|
1.0
|
|
NE2
|
B:HIS103
|
4.4
|
25.4
|
1.0
|
|
CA
|
B:HIS448
|
4.4
|
23.9
|
1.0
|
|
C
|
B:HIS103
|
4.5
|
24.3
|
1.0
|
|
O
|
B:HOH711
|
4.5
|
21.7
|
1.0
|
|
N
|
B:HIS103
|
4.5
|
22.9
|
1.0
|
|
CB
|
B:HIS448
|
4.5
|
24.0
|
1.0
|
|
O
|
B:TRP102
|
4.7
|
22.6
|
1.0
|
|
O
|
B:HOH715
|
4.8
|
17.5
|
1.0
|
|
C
|
B:TRP102
|
4.9
|
22.8
|
1.0
|
|
N
|
B:HIS448
|
4.9
|
23.8
|
1.0
|
|
NE2
|
B:HIS499
|
4.9
|
27.5
|
1.0
|
|
NE2
|
B:HIS141
|
5.0
|
26.2
|
1.0
|
|
Copper binding site 7 out
of 8 in 2yxv
Go back to
Copper Binding Sites List in 2yxv
Copper binding site 7 out
of 8 in the The Deletion Mutant of Multicopper Oxidase Cueo
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 7 of The Deletion Mutant of Multicopper Oxidase Cueo within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu702
b:33.0
occ:1.00
|
CU2
|
B:C2O702
|
0.0
|
33.0
|
1.0
|
|
O1
|
B:C2O702
|
2.0
|
32.8
|
1.0
|
|
NE2
|
B:HIS499
|
2.0
|
27.5
|
1.0
|
|
NE2
|
B:HIS143
|
2.1
|
28.6
|
1.0
|
|
NE2
|
B:HIS448
|
2.1
|
26.6
|
1.0
|
|
CE1
|
B:HIS448
|
2.9
|
26.1
|
1.0
|
|
CE1
|
B:HIS499
|
2.9
|
27.4
|
1.0
|
|
CD2
|
B:HIS143
|
3.0
|
28.2
|
1.0
|
|
CE1
|
B:HIS143
|
3.1
|
28.3
|
1.0
|
|
CD2
|
B:HIS499
|
3.1
|
25.6
|
1.0
|
|
CD2
|
B:HIS448
|
3.2
|
24.2
|
1.0
|
|
CU
|
B:CU703
|
3.5
|
38.4
|
1.0
|
|
CD2
|
B:HIS446
|
3.5
|
24.5
|
1.0
|
|
CU3
|
B:C2O702
|
3.8
|
29.5
|
1.0
|
|
NE2
|
B:HIS101
|
3.9
|
28.9
|
1.0
|
|
CD2
|
B:HIS101
|
4.0
|
27.9
|
1.0
|
|
NE2
|
B:HIS446
|
4.0
|
26.1
|
1.0
|
|
ND1
|
B:HIS499
|
4.1
|
25.4
|
1.0
|
|
ND1
|
B:HIS448
|
4.1
|
25.0
|
1.0
|
|
ND1
|
B:HIS143
|
4.2
|
27.6
|
1.0
|
|
CG
|
B:HIS143
|
4.2
|
25.8
|
1.0
|
|
CG
|
B:HIS499
|
4.2
|
24.4
|
1.0
|
|
CG
|
B:HIS448
|
4.2
|
24.2
|
1.0
|
|
CE1
|
B:HIS141
|
4.3
|
26.4
|
1.0
|
|
CD2
|
B:HIS501
|
4.6
|
23.5
|
1.0
|
|
NE2
|
B:HIS501
|
4.6
|
22.2
|
1.0
|
|
CE1
|
B:HIS101
|
4.6
|
27.5
|
1.0
|
|
NE2
|
B:HIS141
|
4.6
|
26.2
|
1.0
|
|
CG
|
B:HIS101
|
4.7
|
24.8
|
1.0
|
|
CG
|
B:HIS446
|
4.7
|
24.4
|
1.0
|
|
OE2
|
B:GLU506
|
4.9
|
33.9
|
1.0
|
|
CB
|
B:MET497
|
4.9
|
23.8
|
1.0
|
|
OE1
|
B:GLU506
|
4.9
|
31.9
|
1.0
|
|
Copper binding site 8 out
of 8 in 2yxv
Go back to
Copper Binding Sites List in 2yxv
Copper binding site 8 out
of 8 in the The Deletion Mutant of Multicopper Oxidase Cueo
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 8 of The Deletion Mutant of Multicopper Oxidase Cueo within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu702
b:29.5
occ:1.00
|
CU3
|
B:C2O702
|
0.0
|
29.5
|
1.0
|
|
O1
|
B:C2O702
|
2.0
|
32.8
|
1.0
|
|
ND1
|
B:HIS103
|
2.0
|
26.3
|
1.0
|
|
NE2
|
B:HIS501
|
2.0
|
22.2
|
1.0
|
|
NE2
|
B:HIS141
|
2.0
|
26.2
|
1.0
|
|
CE1
|
B:HIS103
|
2.9
|
23.3
|
1.0
|
|
CE1
|
B:HIS141
|
2.9
|
26.4
|
1.0
|
|
CD2
|
B:HIS501
|
2.9
|
23.5
|
1.0
|
|
CE1
|
B:HIS501
|
3.1
|
25.2
|
1.0
|
|
CD2
|
B:HIS141
|
3.1
|
24.5
|
1.0
|
|
CG
|
B:HIS103
|
3.1
|
24.9
|
1.0
|
|
CB
|
B:HIS103
|
3.6
|
24.2
|
1.0
|
|
CU2
|
B:C2O702
|
3.8
|
33.0
|
1.0
|
|
CU
|
B:CU703
|
3.9
|
38.4
|
1.0
|
|
CD2
|
B:HIS101
|
4.0
|
27.9
|
1.0
|
|
CD2
|
B:HIS446
|
4.0
|
24.5
|
1.0
|
|
ND1
|
B:HIS141
|
4.1
|
25.3
|
1.0
|
|
NE2
|
B:HIS103
|
4.1
|
25.4
|
1.0
|
|
CZ2
|
B:TRP139
|
4.1
|
24.3
|
1.0
|
|
CG
|
B:HIS501
|
4.1
|
22.1
|
1.0
|
|
NE2
|
B:HIS446
|
4.1
|
26.1
|
1.0
|
|
ND1
|
B:HIS501
|
4.2
|
23.1
|
1.0
|
|
CD2
|
B:HIS103
|
4.2
|
25.5
|
1.0
|
|
CG
|
B:HIS141
|
4.2
|
24.1
|
1.0
|
|
NE2
|
B:HIS101
|
4.3
|
28.9
|
1.0
|
|
CE2
|
B:TRP139
|
4.5
|
25.3
|
1.0
|
|
NE1
|
B:TRP139
|
4.6
|
24.4
|
1.0
|
|
CA
|
B:HIS103
|
4.7
|
24.0
|
1.0
|
|
CE1
|
B:HIS499
|
4.8
|
27.4
|
1.0
|
|
CH2
|
B:TRP139
|
4.8
|
24.1
|
1.0
|
|
NE2
|
B:HIS499
|
4.8
|
27.5
|
1.0
|
|
CG
|
B:HIS446
|
4.9
|
24.4
|
1.0
|
|
NE2
|
B:HIS143
|
4.9
|
28.6
|
1.0
|
|
CE1
|
B:HIS446
|
5.0
|
25.0
|
1.0
|
|
Reference:
K.Kataoka,
H.Komori,
Y.Ueki,
Y.Konno,
Y.Kamitaka,
S.Kurose,
S.Tsujimura,
Y.Higuchi,
K.Kano,
D.Seo,
T.Sakurai.
Structure and Function of the Engineered Multicopper Oxidase Cueo From Escherichia Coli--Deletion of the Methionine-Rich Helical Region Covering the Substrate-Binding Site J.Mol.Biol. V. 373 141 2007.
ISSN: ISSN 0022-2836
PubMed: 17804014
DOI: 10.1016/J.JMB.2007.07.041
Page generated: Wed Jul 31 00:26:07 2024
|
