Copper in PDB 6iqy: High Resolution Structure of Bilirubin Oxidase From Myrothecium Verrucaria - M467Q Mutant, Anaerobically Prepared
Enzymatic activity of High Resolution Structure of Bilirubin Oxidase From Myrothecium Verrucaria - M467Q Mutant, Anaerobically Prepared
All present enzymatic activity of High Resolution Structure of Bilirubin Oxidase From Myrothecium Verrucaria - M467Q Mutant, Anaerobically Prepared:
1.3.3.5;
Protein crystallography data
The structure of High Resolution Structure of Bilirubin Oxidase From Myrothecium Verrucaria - M467Q Mutant, Anaerobically Prepared, PDB code: 6iqy
was solved by
N.Shibata,
M.Akter,
Y.Higuchi,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
45.86 /
1.60
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
59.298,
152.253,
69.908,
90.00,
91.66,
90.00
|
R / Rfree (%)
|
19.1 /
22.5
|
Other elements in 6iqy:
The structure of High Resolution Structure of Bilirubin Oxidase From Myrothecium Verrucaria - M467Q Mutant, Anaerobically Prepared also contains other interesting chemical elements:
Copper Binding Sites:
The binding sites of Copper atom in the High Resolution Structure of Bilirubin Oxidase From Myrothecium Verrucaria - M467Q Mutant, Anaerobically Prepared
(pdb code 6iqy). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 8 binding sites of Copper where determined in the
High Resolution Structure of Bilirubin Oxidase From Myrothecium Verrucaria - M467Q Mutant, Anaerobically Prepared, PDB code: 6iqy:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Copper binding site 1 out
of 8 in 6iqy
Go back to
Copper Binding Sites List in 6iqy
Copper binding site 1 out
of 8 in the High Resolution Structure of Bilirubin Oxidase From Myrothecium Verrucaria - M467Q Mutant, Anaerobically Prepared
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of High Resolution Structure of Bilirubin Oxidase From Myrothecium Verrucaria - M467Q Mutant, Anaerobically Prepared within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu601
b:9.7
occ:0.97
|
ND1
|
A:HIS462
|
2.0
|
10.6
|
1.0
|
ND1
|
A:HIS398
|
2.0
|
6.9
|
1.0
|
SG
|
A:CYS457
|
2.2
|
9.4
|
1.0
|
OE1
|
A:GLN467
|
2.7
|
9.2
|
1.0
|
CE1
|
A:HIS398
|
3.0
|
11.7
|
1.0
|
CG
|
A:HIS462
|
3.0
|
8.0
|
1.0
|
CE1
|
A:HIS462
|
3.0
|
11.2
|
1.0
|
CG
|
A:HIS398
|
3.0
|
10.4
|
1.0
|
CB
|
A:CYS457
|
3.2
|
13.1
|
1.0
|
CB
|
A:HIS462
|
3.3
|
9.3
|
1.0
|
CB
|
A:HIS398
|
3.4
|
8.9
|
1.0
|
O
|
A:THR397
|
3.6
|
11.0
|
1.0
|
CA
|
A:HIS398
|
3.7
|
9.5
|
1.0
|
CD
|
A:GLN467
|
3.8
|
14.5
|
1.0
|
CB
|
A:ASN459
|
4.1
|
10.8
|
1.0
|
NE2
|
A:HIS398
|
4.1
|
19.6
|
1.0
|
NE2
|
A:HIS462
|
4.1
|
9.0
|
1.0
|
CD2
|
A:HIS462
|
4.1
|
9.8
|
1.0
|
O
|
A:HOH716
|
4.1
|
10.7
|
1.0
|
CD2
|
A:HIS398
|
4.1
|
17.7
|
1.0
|
C
|
A:THR397
|
4.4
|
11.1
|
1.0
|
NE2
|
A:GLN467
|
4.4
|
12.4
|
1.0
|
N
|
A:HIS398
|
4.5
|
9.3
|
1.0
|
CA
|
A:CYS457
|
4.6
|
9.9
|
1.0
|
CD
|
A:PRO399
|
4.8
|
9.0
|
1.0
|
CA
|
A:HIS462
|
4.8
|
7.9
|
1.0
|
C
|
A:HIS398
|
4.8
|
8.1
|
1.0
|
CG
|
A:ASN459
|
4.9
|
9.0
|
1.0
|
CG
|
A:GLN467
|
5.0
|
10.2
|
1.0
|
N
|
A:ASN459
|
5.0
|
10.8
|
1.0
|
|
Copper binding site 2 out
of 8 in 6iqy
Go back to
Copper Binding Sites List in 6iqy
Copper binding site 2 out
of 8 in the High Resolution Structure of Bilirubin Oxidase From Myrothecium Verrucaria - M467Q Mutant, Anaerobically Prepared
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of High Resolution Structure of Bilirubin Oxidase From Myrothecium Verrucaria - M467Q Mutant, Anaerobically Prepared within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu602
b:12.5
occ:0.98
|
ND1
|
A:HIS96
|
2.0
|
8.8
|
1.0
|
NE2
|
A:HIS134
|
2.0
|
10.5
|
1.0
|
NE2
|
A:HIS458
|
2.2
|
8.8
|
1.0
|
O
|
A:HOH1215
|
2.6
|
23.6
|
1.0
|
CE1
|
A:HIS96
|
2.8
|
8.3
|
1.0
|
CE1
|
A:HIS134
|
2.9
|
15.3
|
1.0
|
CD2
|
A:HIS134
|
3.0
|
8.3
|
1.0
|
CG
|
A:HIS96
|
3.1
|
9.3
|
1.0
|
CE1
|
A:HIS458
|
3.1
|
11.3
|
1.0
|
CD2
|
A:HIS458
|
3.2
|
11.8
|
1.0
|
CB
|
A:HIS96
|
3.5
|
6.7
|
1.0
|
CZ2
|
A:TRP132
|
3.6
|
9.4
|
1.0
|
CE2
|
A:TRP132
|
3.9
|
9.7
|
1.0
|
CD2
|
A:HIS94
|
4.0
|
10.8
|
1.0
|
NE1
|
A:TRP132
|
4.0
|
10.4
|
1.0
|
NE2
|
A:HIS96
|
4.0
|
9.6
|
1.0
|
ND1
|
A:HIS134
|
4.0
|
11.4
|
1.0
|
CG
|
A:HIS134
|
4.1
|
11.9
|
1.0
|
CD2
|
A:HIS96
|
4.1
|
8.0
|
1.0
|
CU
|
A:CU604
|
4.2
|
15.7
|
0.7
|
ND1
|
A:HIS458
|
4.2
|
9.3
|
1.0
|
CB
|
A:ALA274
|
4.2
|
9.9
|
1.0
|
CG
|
A:HIS458
|
4.3
|
7.4
|
1.0
|
CH2
|
A:TRP132
|
4.4
|
10.4
|
1.0
|
CD2
|
A:HIS401
|
4.4
|
9.2
|
1.0
|
O
|
A:HOH893
|
4.4
|
25.2
|
1.0
|
NE2
|
A:HIS94
|
4.6
|
9.4
|
1.0
|
NE2
|
A:HIS401
|
4.6
|
7.9
|
1.0
|
CA
|
A:HIS96
|
4.8
|
4.7
|
1.0
|
CU
|
A:CU603
|
4.8
|
11.2
|
0.8
|
CD2
|
A:TRP132
|
4.9
|
10.3
|
1.0
|
|
Copper binding site 3 out
of 8 in 6iqy
Go back to
Copper Binding Sites List in 6iqy
Copper binding site 3 out
of 8 in the High Resolution Structure of Bilirubin Oxidase From Myrothecium Verrucaria - M467Q Mutant, Anaerobically Prepared
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of High Resolution Structure of Bilirubin Oxidase From Myrothecium Verrucaria - M467Q Mutant, Anaerobically Prepared within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu603
b:11.2
occ:0.79
|
NE2
|
A:HIS403
|
1.9
|
9.9
|
1.0
|
NE2
|
A:HIS136
|
2.0
|
10.2
|
1.0
|
NE2
|
A:HIS456
|
2.0
|
9.8
|
1.0
|
O
|
A:HOH1215
|
2.2
|
23.6
|
1.0
|
CE1
|
A:HIS403
|
2.8
|
11.0
|
1.0
|
CD2
|
A:HIS456
|
3.0
|
4.3
|
1.0
|
CD2
|
A:HIS136
|
3.0
|
10.7
|
1.0
|
CE1
|
A:HIS456
|
3.0
|
7.4
|
1.0
|
CE1
|
A:HIS136
|
3.0
|
14.4
|
1.0
|
CD2
|
A:HIS403
|
3.1
|
11.1
|
1.0
|
CD2
|
A:HIS401
|
3.7
|
9.2
|
1.0
|
ND1
|
A:HIS403
|
4.0
|
12.7
|
1.0
|
CU
|
A:CU604
|
4.0
|
15.7
|
0.7
|
CD2
|
A:HIS94
|
4.0
|
10.8
|
1.0
|
ND1
|
A:HIS456
|
4.1
|
8.9
|
1.0
|
ND1
|
A:HIS136
|
4.1
|
12.9
|
1.0
|
CG
|
A:HIS456
|
4.1
|
9.4
|
1.0
|
CG
|
A:HIS403
|
4.1
|
10.6
|
1.0
|
CG
|
A:HIS136
|
4.1
|
10.2
|
1.0
|
CE
|
A:MET454
|
4.2
|
11.4
|
1.0
|
O
|
A:HOH893
|
4.2
|
25.2
|
1.0
|
NE2
|
A:HIS94
|
4.3
|
9.4
|
1.0
|
O
|
A:HOH755
|
4.3
|
28.9
|
1.0
|
NE2
|
A:HIS401
|
4.4
|
7.9
|
1.0
|
CE
|
A:MET468
|
4.6
|
12.2
|
0.5
|
CG
|
A:HIS94
|
4.8
|
5.3
|
1.0
|
CU
|
A:CU602
|
4.8
|
12.5
|
1.0
|
CG
|
A:HIS401
|
4.8
|
10.8
|
1.0
|
OE2
|
A:GLU463
|
4.8
|
12.9
|
1.0
|
CB
|
A:MET454
|
4.9
|
11.8
|
1.0
|
NE2
|
A:HIS458
|
4.9
|
8.8
|
1.0
|
CD2
|
A:HIS458
|
4.9
|
11.8
|
1.0
|
|
Copper binding site 4 out
of 8 in 6iqy
Go back to
Copper Binding Sites List in 6iqy
Copper binding site 4 out
of 8 in the High Resolution Structure of Bilirubin Oxidase From Myrothecium Verrucaria - M467Q Mutant, Anaerobically Prepared
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of High Resolution Structure of Bilirubin Oxidase From Myrothecium Verrucaria - M467Q Mutant, Anaerobically Prepared within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu604
b:15.7
occ:0.70
|
NE2
|
A:HIS401
|
1.8
|
7.9
|
1.0
|
NE2
|
A:HIS94
|
1.9
|
9.4
|
1.0
|
CD2
|
A:HIS401
|
2.7
|
9.2
|
1.0
|
O
|
A:HOH1156
|
2.8
|
14.1
|
1.0
|
CD2
|
A:HIS94
|
2.8
|
10.8
|
1.0
|
CE1
|
A:HIS401
|
2.9
|
14.2
|
1.0
|
CE1
|
A:HIS94
|
2.9
|
15.1
|
1.0
|
NE2
|
A:HIS403
|
3.3
|
9.9
|
1.0
|
O
|
A:HOH1215
|
3.3
|
23.6
|
1.0
|
ND1
|
A:HIS96
|
3.4
|
8.8
|
1.0
|
CE1
|
A:HIS403
|
3.5
|
11.0
|
1.0
|
CG
|
A:HIS96
|
3.5
|
9.3
|
1.0
|
CD2
|
A:HIS403
|
3.5
|
11.1
|
1.0
|
CE1
|
A:HIS96
|
3.7
|
8.3
|
1.0
|
ND1
|
A:HIS403
|
3.7
|
12.7
|
1.0
|
CG
|
A:HIS403
|
3.7
|
10.6
|
1.0
|
CD2
|
A:HIS96
|
3.8
|
8.0
|
1.0
|
CG
|
A:HIS401
|
3.9
|
10.8
|
1.0
|
CA
|
A:HIS96
|
3.9
|
4.7
|
1.0
|
ND1
|
A:HIS401
|
3.9
|
8.0
|
1.0
|
NE2
|
A:HIS96
|
3.9
|
9.6
|
1.0
|
CG
|
A:HIS94
|
4.0
|
5.3
|
1.0
|
CB
|
A:HIS96
|
4.0
|
6.7
|
1.0
|
ND1
|
A:HIS94
|
4.0
|
8.0
|
1.0
|
CU
|
A:CU603
|
4.0
|
11.2
|
0.8
|
CU
|
A:CU602
|
4.2
|
12.5
|
1.0
|
N
|
A:GLY97
|
4.6
|
10.2
|
1.0
|
O
|
A:HOH809
|
4.6
|
13.9
|
1.0
|
CA
|
A:HIS403
|
4.6
|
11.4
|
1.0
|
O
|
A:HOH852
|
4.6
|
11.1
|
1.0
|
CB
|
A:HIS403
|
4.7
|
8.8
|
1.0
|
C
|
A:HIS96
|
4.8
|
11.6
|
1.0
|
N
|
A:HIS96
|
4.8
|
6.6
|
1.0
|
|
Copper binding site 5 out
of 8 in 6iqy
Go back to
Copper Binding Sites List in 6iqy
Copper binding site 5 out
of 8 in the High Resolution Structure of Bilirubin Oxidase From Myrothecium Verrucaria - M467Q Mutant, Anaerobically Prepared
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 5 of High Resolution Structure of Bilirubin Oxidase From Myrothecium Verrucaria - M467Q Mutant, Anaerobically Prepared within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu601
b:10.3
occ:0.97
|
ND1
|
B:HIS398
|
2.0
|
8.9
|
1.0
|
ND1
|
B:HIS462
|
2.1
|
9.9
|
1.0
|
SG
|
B:CYS457
|
2.3
|
10.2
|
1.0
|
OE1
|
B:GLN467
|
2.7
|
9.9
|
1.0
|
CE1
|
B:HIS398
|
3.0
|
16.8
|
1.0
|
CG
|
B:HIS462
|
3.0
|
9.8
|
1.0
|
CG
|
B:HIS398
|
3.0
|
10.1
|
1.0
|
CE1
|
B:HIS462
|
3.1
|
13.1
|
1.0
|
CB
|
B:CYS457
|
3.2
|
11.9
|
1.0
|
CB
|
B:HIS462
|
3.3
|
11.9
|
1.0
|
CB
|
B:HIS398
|
3.4
|
11.9
|
1.0
|
O
|
B:THR397
|
3.6
|
9.7
|
1.0
|
CA
|
B:HIS398
|
3.7
|
9.5
|
1.0
|
CD
|
B:GLN467
|
3.8
|
12.9
|
1.0
|
O
|
B:HOH723
|
4.0
|
9.5
|
1.0
|
CB
|
B:ASN459
|
4.1
|
7.5
|
1.0
|
NE2
|
B:HIS398
|
4.1
|
25.4
|
1.0
|
CD2
|
B:HIS398
|
4.2
|
18.4
|
1.0
|
CD2
|
B:HIS462
|
4.2
|
11.3
|
1.0
|
NE2
|
B:HIS462
|
4.2
|
9.7
|
1.0
|
C
|
B:THR397
|
4.4
|
10.3
|
1.0
|
NE2
|
B:GLN467
|
4.4
|
11.2
|
1.0
|
N
|
B:HIS398
|
4.5
|
8.8
|
1.0
|
CA
|
B:CYS457
|
4.6
|
10.9
|
1.0
|
CA
|
B:HIS462
|
4.8
|
8.9
|
1.0
|
CD
|
B:PRO399
|
4.8
|
10.3
|
1.0
|
C
|
B:HIS398
|
4.8
|
7.5
|
1.0
|
CG
|
B:ASN459
|
4.9
|
9.8
|
1.0
|
N
|
B:ASN459
|
5.0
|
8.9
|
1.0
|
|
Copper binding site 6 out
of 8 in 6iqy
Go back to
Copper Binding Sites List in 6iqy
Copper binding site 6 out
of 8 in the High Resolution Structure of Bilirubin Oxidase From Myrothecium Verrucaria - M467Q Mutant, Anaerobically Prepared
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 6 of High Resolution Structure of Bilirubin Oxidase From Myrothecium Verrucaria - M467Q Mutant, Anaerobically Prepared within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu602
b:11.9
occ:0.92
|
NE2
|
B:HIS134
|
2.0
|
10.5
|
1.0
|
ND1
|
B:HIS96
|
2.0
|
7.6
|
1.0
|
NE2
|
B:HIS458
|
2.2
|
7.5
|
1.0
|
O
|
B:HOH1235
|
2.6
|
23.9
|
1.0
|
CE1
|
B:HIS96
|
2.9
|
8.2
|
1.0
|
CE1
|
B:HIS134
|
2.9
|
13.6
|
1.0
|
CD2
|
B:HIS134
|
3.0
|
8.2
|
1.0
|
CE1
|
B:HIS458
|
3.0
|
9.5
|
1.0
|
CG
|
B:HIS96
|
3.1
|
9.0
|
1.0
|
CD2
|
B:HIS458
|
3.2
|
11.2
|
1.0
|
CB
|
B:HIS96
|
3.5
|
7.9
|
1.0
|
CZ2
|
B:TRP132
|
3.6
|
9.0
|
1.0
|
CD2
|
B:HIS94
|
3.9
|
9.3
|
1.0
|
CE2
|
B:TRP132
|
3.9
|
8.4
|
1.0
|
NE1
|
B:TRP132
|
3.9
|
9.0
|
1.0
|
ND1
|
B:HIS134
|
4.0
|
12.6
|
1.0
|
NE2
|
B:HIS96
|
4.1
|
8.8
|
1.0
|
CG
|
B:HIS134
|
4.1
|
10.5
|
1.0
|
CD2
|
B:HIS96
|
4.1
|
7.1
|
1.0
|
CU
|
B:CU604
|
4.2
|
16.1
|
0.7
|
O
|
B:HOH1069
|
4.2
|
25.0
|
1.0
|
ND1
|
B:HIS458
|
4.2
|
12.4
|
1.0
|
CB
|
B:ALA274
|
4.3
|
9.2
|
1.0
|
CG
|
B:HIS458
|
4.3
|
7.9
|
1.0
|
CD2
|
B:HIS401
|
4.4
|
10.9
|
1.0
|
CH2
|
B:TRP132
|
4.4
|
10.3
|
1.0
|
NE2
|
B:HIS94
|
4.4
|
9.2
|
1.0
|
NE2
|
B:HIS401
|
4.5
|
10.7
|
1.0
|
CA
|
B:HIS96
|
4.8
|
4.4
|
1.0
|
CU
|
B:CU603
|
4.8
|
11.5
|
0.8
|
CD2
|
B:TRP132
|
4.9
|
10.8
|
1.0
|
CD1
|
B:TRP132
|
5.0
|
7.0
|
1.0
|
|
Copper binding site 7 out
of 8 in 6iqy
Go back to
Copper Binding Sites List in 6iqy
Copper binding site 7 out
of 8 in the High Resolution Structure of Bilirubin Oxidase From Myrothecium Verrucaria - M467Q Mutant, Anaerobically Prepared
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 7 of High Resolution Structure of Bilirubin Oxidase From Myrothecium Verrucaria - M467Q Mutant, Anaerobically Prepared within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu603
b:11.5
occ:0.79
|
NE2
|
B:HIS403
|
1.9
|
8.1
|
1.0
|
NE2
|
B:HIS136
|
2.0
|
13.1
|
1.0
|
NE2
|
B:HIS456
|
2.1
|
8.2
|
1.0
|
O
|
B:HOH1235
|
2.2
|
23.9
|
1.0
|
CE1
|
B:HIS403
|
2.8
|
10.0
|
1.0
|
CD2
|
B:HIS136
|
3.0
|
14.3
|
1.0
|
CE1
|
B:HIS456
|
3.0
|
9.7
|
1.0
|
CD2
|
B:HIS456
|
3.0
|
6.2
|
1.0
|
CE1
|
B:HIS136
|
3.1
|
13.1
|
1.0
|
CD2
|
B:HIS403
|
3.1
|
9.4
|
1.0
|
CD2
|
B:HIS401
|
3.6
|
10.9
|
1.0
|
ND1
|
B:HIS403
|
4.0
|
13.6
|
1.0
|
CU
|
B:CU604
|
4.0
|
16.1
|
0.7
|
ND1
|
B:HIS456
|
4.1
|
11.9
|
1.0
|
CG
|
B:HIS403
|
4.1
|
10.4
|
1.0
|
CG
|
B:HIS136
|
4.1
|
9.9
|
1.0
|
CD2
|
B:HIS94
|
4.1
|
9.3
|
1.0
|
CG
|
B:HIS456
|
4.1
|
11.0
|
1.0
|
ND1
|
B:HIS136
|
4.1
|
11.6
|
1.0
|
O
|
B:HOH1069
|
4.2
|
25.0
|
1.0
|
CE
|
B:MET454
|
4.2
|
10.3
|
1.0
|
O
|
B:HOH716
|
4.2
|
17.1
|
1.0
|
NE2
|
B:HIS401
|
4.3
|
10.7
|
1.0
|
NE2
|
B:HIS94
|
4.4
|
9.2
|
1.0
|
CE
|
B:MET468
|
4.7
|
13.3
|
0.3
|
CG
|
B:HIS94
|
4.8
|
5.9
|
1.0
|
CU
|
B:CU602
|
4.8
|
11.9
|
0.9
|
CG
|
B:HIS401
|
4.8
|
9.1
|
1.0
|
OE2
|
B:GLU463
|
4.8
|
15.2
|
1.0
|
NE2
|
B:HIS458
|
4.8
|
7.5
|
1.0
|
CB
|
B:MET454
|
4.9
|
12.4
|
1.0
|
CD2
|
B:HIS458
|
4.9
|
11.2
|
1.0
|
|
Copper binding site 8 out
of 8 in 6iqy
Go back to
Copper Binding Sites List in 6iqy
Copper binding site 8 out
of 8 in the High Resolution Structure of Bilirubin Oxidase From Myrothecium Verrucaria - M467Q Mutant, Anaerobically Prepared
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 8 of High Resolution Structure of Bilirubin Oxidase From Myrothecium Verrucaria - M467Q Mutant, Anaerobically Prepared within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu604
b:16.1
occ:0.73
|
NE2
|
B:HIS401
|
1.8
|
10.7
|
1.0
|
NE2
|
B:HIS94
|
1.9
|
9.2
|
1.0
|
CD2
|
B:HIS401
|
2.8
|
10.9
|
1.0
|
CE1
|
B:HIS401
|
2.8
|
17.3
|
1.0
|
CE1
|
B:HIS94
|
2.9
|
13.0
|
1.0
|
CD2
|
B:HIS94
|
2.9
|
9.3
|
1.0
|
O
|
B:HOH1143
|
2.9
|
15.8
|
1.0
|
O
|
B:HOH1235
|
3.1
|
23.9
|
1.0
|
NE2
|
B:HIS403
|
3.2
|
8.1
|
1.0
|
CE1
|
B:HIS403
|
3.4
|
10.0
|
1.0
|
ND1
|
B:HIS96
|
3.4
|
7.6
|
1.0
|
CG
|
B:HIS96
|
3.5
|
9.0
|
1.0
|
CD2
|
B:HIS403
|
3.5
|
9.4
|
1.0
|
ND1
|
B:HIS403
|
3.7
|
13.6
|
1.0
|
CG
|
B:HIS403
|
3.8
|
10.4
|
1.0
|
CE1
|
B:HIS96
|
3.8
|
8.2
|
1.0
|
CA
|
B:HIS96
|
3.9
|
4.4
|
1.0
|
CD2
|
B:HIS96
|
3.9
|
7.1
|
1.0
|
ND1
|
B:HIS401
|
3.9
|
7.6
|
1.0
|
CG
|
B:HIS401
|
3.9
|
9.1
|
1.0
|
CB
|
B:HIS96
|
3.9
|
7.9
|
1.0
|
ND1
|
B:HIS94
|
3.9
|
5.4
|
1.0
|
CG
|
B:HIS94
|
4.0
|
5.9
|
1.0
|
CU
|
B:CU603
|
4.0
|
11.5
|
0.8
|
NE2
|
B:HIS96
|
4.0
|
8.8
|
1.0
|
CU
|
B:CU602
|
4.2
|
11.9
|
0.9
|
N
|
B:GLY97
|
4.6
|
8.8
|
1.0
|
CA
|
B:HIS403
|
4.6
|
10.5
|
1.0
|
CB
|
B:HIS403
|
4.7
|
9.6
|
1.0
|
O
|
B:HOH761
|
4.7
|
12.0
|
1.0
|
O
|
B:HOH776
|
4.7
|
10.9
|
1.0
|
C
|
B:HIS96
|
4.8
|
8.8
|
1.0
|
N
|
B:HIS96
|
4.8
|
6.2
|
1.0
|
|
Reference:
M.Akter,
T.Tokiwa,
M.Shoji,
K.Nishikawa,
Y.Shigeta,
T.Sakurai,
Y.Higuchi,
K.Kataoka,
N.Shibata.
Redox Potential-Dependent Formation of An Unusual His-Trp Bond in Bilirubin Oxidase. Chemistry V. 24 18052 2018.
ISSN: ISSN 1521-3765
PubMed: 30156345
DOI: 10.1002/CHEM.201803798
Page generated: Wed Jul 31 06:19:20 2024
|