Copper in PDB 6i3k: Bilirubin Oxidase From Myrothecium Verrucaria, Mutant W396A in Complex with Ferricyanide
Enzymatic activity of Bilirubin Oxidase From Myrothecium Verrucaria, Mutant W396A in Complex with Ferricyanide
All present enzymatic activity of Bilirubin Oxidase From Myrothecium Verrucaria, Mutant W396A in Complex with Ferricyanide:
1.3.3.5;
Protein crystallography data
The structure of Bilirubin Oxidase From Myrothecium Verrucaria, Mutant W396A in Complex with Ferricyanide, PDB code: 6i3k
was solved by
T.Koval,
L.Svecova,
T.Skalova,
P.Kolenko,
J.Duskova,
L.H.Ostergaard,
J.Dohnalek,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
47.93 /
1.60
|
Space group
|
F 2 2 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
136.906,
201.803,
217.869,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
13.1 /
15.4
|
Other elements in 6i3k:
The structure of Bilirubin Oxidase From Myrothecium Verrucaria, Mutant W396A in Complex with Ferricyanide also contains other interesting chemical elements:
Copper Binding Sites:
The binding sites of Copper atom in the Bilirubin Oxidase From Myrothecium Verrucaria, Mutant W396A in Complex with Ferricyanide
(pdb code 6i3k). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 8 binding sites of Copper where determined in the
Bilirubin Oxidase From Myrothecium Verrucaria, Mutant W396A in Complex with Ferricyanide, PDB code: 6i3k:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Copper binding site 1 out
of 8 in 6i3k
Go back to
Copper Binding Sites List in 6i3k
Copper binding site 1 out
of 8 in the Bilirubin Oxidase From Myrothecium Verrucaria, Mutant W396A in Complex with Ferricyanide
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Bilirubin Oxidase From Myrothecium Verrucaria, Mutant W396A in Complex with Ferricyanide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu601
b:10.9
occ:1.00
|
ND1
|
A:HIS398
|
2.0
|
10.4
|
1.0
|
ND1
|
A:HIS462
|
2.0
|
10.6
|
1.0
|
SG
|
A:CYS457
|
2.2
|
10.3
|
1.0
|
CE1
|
A:HIS398
|
2.9
|
10.6
|
1.0
|
CE1
|
A:HIS462
|
3.0
|
11.2
|
1.0
|
CG
|
A:HIS462
|
3.0
|
11.0
|
1.0
|
CG
|
A:HIS398
|
3.0
|
10.0
|
1.0
|
CB
|
A:CYS457
|
3.2
|
9.9
|
1.0
|
CB
|
A:HIS462
|
3.3
|
10.6
|
1.0
|
CB
|
A:HIS398
|
3.4
|
9.9
|
1.0
|
SD
|
A:MET467
|
3.4
|
12.3
|
1.0
|
O
|
A:THR397
|
3.5
|
10.3
|
1.0
|
CA
|
A:HIS398
|
3.6
|
9.8
|
1.0
|
CB
|
A:ASN459
|
4.0
|
9.4
|
1.0
|
NE2
|
A:HIS398
|
4.1
|
11.4
|
1.0
|
CD2
|
A:HIS398
|
4.1
|
11.4
|
1.0
|
NE2
|
A:HIS462
|
4.2
|
11.5
|
1.0
|
CD2
|
A:HIS462
|
4.2
|
11.5
|
1.0
|
C
|
A:THR397
|
4.2
|
10.0
|
1.0
|
N
|
A:HIS398
|
4.4
|
10.1
|
1.0
|
CE
|
A:MET467
|
4.4
|
11.7
|
1.0
|
CA
|
A:CYS457
|
4.6
|
9.7
|
1.0
|
CD
|
A:PRO399
|
4.8
|
9.1
|
1.0
|
C
|
A:HIS398
|
4.8
|
9.0
|
1.0
|
CA
|
A:HIS462
|
4.8
|
10.5
|
1.0
|
CG
|
A:ASN459
|
4.8
|
10.0
|
1.0
|
N
|
A:ASN459
|
5.0
|
9.1
|
1.0
|
ND2
|
A:ASN459
|
5.0
|
9.4
|
1.0
|
CG
|
A:MET467
|
5.0
|
11.4
|
1.0
|
|
Copper binding site 2 out
of 8 in 6i3k
Go back to
Copper Binding Sites List in 6i3k
Copper binding site 2 out
of 8 in the Bilirubin Oxidase From Myrothecium Verrucaria, Mutant W396A in Complex with Ferricyanide
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Bilirubin Oxidase From Myrothecium Verrucaria, Mutant W396A in Complex with Ferricyanide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu602
b:11.2
occ:1.00
|
NE2
|
A:HIS403
|
2.0
|
9.5
|
1.0
|
NE2
|
A:HIS136
|
2.0
|
11.2
|
1.0
|
NE2
|
A:HIS456
|
2.0
|
8.6
|
1.0
|
O
|
A:HOH1122
|
2.4
|
29.5
|
0.5
|
CD2
|
A:HIS456
|
2.9
|
8.9
|
1.0
|
CE1
|
A:HIS403
|
2.9
|
9.5
|
1.0
|
CE1
|
A:HIS136
|
2.9
|
12.5
|
1.0
|
CE1
|
A:HIS456
|
3.0
|
9.2
|
1.0
|
CD2
|
A:HIS403
|
3.0
|
9.1
|
1.0
|
CD2
|
A:HIS136
|
3.1
|
10.8
|
1.0
|
CD2
|
A:HIS401
|
3.8
|
9.6
|
1.0
|
CE
|
A:MET454
|
4.0
|
11.2
|
1.0
|
CG
|
A:HIS456
|
4.1
|
8.9
|
1.0
|
ND1
|
A:HIS403
|
4.1
|
8.5
|
1.0
|
ND1
|
A:HIS456
|
4.1
|
9.3
|
1.0
|
ND1
|
A:HIS136
|
4.1
|
10.4
|
1.0
|
CG
|
A:HIS403
|
4.1
|
8.8
|
1.0
|
CG
|
A:HIS136
|
4.2
|
9.8
|
1.0
|
CD2
|
A:HIS94
|
4.3
|
9.3
|
1.0
|
CU
|
A:CU604
|
4.3
|
11.6
|
1.0
|
NE2
|
A:HIS401
|
4.4
|
8.2
|
1.0
|
NE2
|
A:HIS94
|
4.5
|
9.4
|
1.0
|
CB
|
A:MET454
|
4.6
|
10.1
|
1.0
|
OE2
|
A:GLU463
|
4.8
|
13.8
|
1.0
|
CG
|
A:HIS94
|
4.9
|
9.2
|
1.0
|
SD
|
A:MET454
|
4.9
|
12.1
|
1.0
|
NE2
|
A:HIS458
|
4.9
|
9.2
|
1.0
|
CG
|
A:HIS401
|
5.0
|
8.6
|
1.0
|
CU
|
A:CU603
|
5.0
|
10.6
|
1.0
|
SD
|
A:MET468
|
5.0
|
10.9
|
0.5
|
CD2
|
A:HIS458
|
5.0
|
9.2
|
1.0
|
|
Copper binding site 3 out
of 8 in 6i3k
Go back to
Copper Binding Sites List in 6i3k
Copper binding site 3 out
of 8 in the Bilirubin Oxidase From Myrothecium Verrucaria, Mutant W396A in Complex with Ferricyanide
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Bilirubin Oxidase From Myrothecium Verrucaria, Mutant W396A in Complex with Ferricyanide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu603
b:10.6
occ:1.00
|
ND1
|
A:HIS96
|
2.0
|
9.0
|
1.0
|
NE2
|
A:HIS134
|
2.0
|
10.5
|
1.0
|
NE2
|
A:HIS458
|
2.1
|
9.2
|
1.0
|
O
|
A:HOH1122
|
2.6
|
29.5
|
0.5
|
CE1
|
A:HIS96
|
2.9
|
8.7
|
1.0
|
CE1
|
A:HIS134
|
3.0
|
11.2
|
1.0
|
CE1
|
A:HIS458
|
3.0
|
9.4
|
1.0
|
CD2
|
A:HIS134
|
3.0
|
10.2
|
1.0
|
CG
|
A:HIS96
|
3.1
|
8.6
|
1.0
|
CD2
|
A:HIS458
|
3.2
|
9.2
|
1.0
|
CB
|
A:HIS96
|
3.4
|
9.1
|
1.0
|
CZ2
|
A:TRP132
|
3.7
|
9.7
|
1.0
|
CD2
|
A:HIS94
|
3.9
|
9.3
|
1.0
|
CE2
|
A:TRP132
|
3.9
|
9.8
|
1.0
|
NE1
|
A:TRP132
|
4.0
|
9.9
|
1.0
|
NE2
|
A:HIS96
|
4.1
|
9.2
|
1.0
|
ND1
|
A:HIS134
|
4.1
|
10.3
|
1.0
|
CG
|
A:HIS134
|
4.1
|
9.8
|
1.0
|
ND1
|
A:HIS458
|
4.2
|
9.6
|
1.0
|
CD2
|
A:HIS96
|
4.2
|
10.0
|
1.0
|
CB
|
A:ALA274
|
4.2
|
8.8
|
1.0
|
CG
|
A:HIS458
|
4.3
|
9.0
|
1.0
|
CU
|
A:CU604
|
4.3
|
11.6
|
1.0
|
NE2
|
A:HIS94
|
4.4
|
9.4
|
1.0
|
CD2
|
A:HIS401
|
4.4
|
9.6
|
1.0
|
CH2
|
A:TRP132
|
4.5
|
10.0
|
1.0
|
NE2
|
A:HIS401
|
4.5
|
8.2
|
1.0
|
CA
|
A:HIS96
|
4.8
|
9.0
|
1.0
|
CD2
|
A:TRP132
|
4.9
|
9.4
|
1.0
|
CD1
|
A:TRP132
|
5.0
|
9.7
|
1.0
|
CU
|
A:CU602
|
5.0
|
11.2
|
1.0
|
|
Copper binding site 4 out
of 8 in 6i3k
Go back to
Copper Binding Sites List in 6i3k
Copper binding site 4 out
of 8 in the Bilirubin Oxidase From Myrothecium Verrucaria, Mutant W396A in Complex with Ferricyanide
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of Bilirubin Oxidase From Myrothecium Verrucaria, Mutant W396A in Complex with Ferricyanide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu604
b:11.6
occ:1.00
|
NE2
|
A:HIS401
|
1.9
|
8.2
|
1.0
|
NE2
|
A:HIS94
|
1.9
|
9.4
|
1.0
|
O
|
A:HOH1210
|
2.7
|
10.4
|
1.0
|
CE1
|
A:HIS94
|
2.8
|
10.0
|
1.0
|
CE1
|
A:HIS401
|
2.9
|
9.2
|
1.0
|
CD2
|
A:HIS401
|
2.9
|
9.6
|
1.0
|
CD2
|
A:HIS94
|
2.9
|
9.3
|
1.0
|
NE2
|
A:HIS403
|
3.3
|
9.5
|
1.0
|
CG
|
A:HIS96
|
3.4
|
8.6
|
1.0
|
ND1
|
A:HIS96
|
3.5
|
9.0
|
1.0
|
CD2
|
A:HIS403
|
3.5
|
9.1
|
1.0
|
CE1
|
A:HIS403
|
3.5
|
9.5
|
1.0
|
CG
|
A:HIS403
|
3.7
|
8.8
|
1.0
|
ND1
|
A:HIS403
|
3.7
|
8.5
|
1.0
|
CA
|
A:HIS96
|
3.8
|
9.0
|
1.0
|
CD2
|
A:HIS96
|
3.8
|
10.0
|
1.0
|
O
|
A:HOH1122
|
3.8
|
29.5
|
0.5
|
CE1
|
A:HIS96
|
3.8
|
8.7
|
1.0
|
CB
|
A:HIS96
|
3.8
|
9.1
|
1.0
|
ND1
|
A:HIS94
|
3.9
|
8.9
|
1.0
|
NE2
|
A:HIS96
|
4.0
|
9.2
|
1.0
|
ND1
|
A:HIS401
|
4.0
|
8.8
|
1.0
|
CG
|
A:HIS94
|
4.0
|
9.2
|
1.0
|
CG
|
A:HIS401
|
4.0
|
8.6
|
1.0
|
CU
|
A:CU603
|
4.3
|
10.6
|
1.0
|
CU
|
A:CU602
|
4.3
|
11.2
|
1.0
|
N
|
A:GLY97
|
4.5
|
9.5
|
1.0
|
O
|
A:HOH1041
|
4.5
|
8.5
|
1.0
|
O
|
A:HOH995
|
4.5
|
8.9
|
1.0
|
CA
|
A:HIS403
|
4.6
|
9.6
|
1.0
|
CB
|
A:HIS403
|
4.6
|
9.2
|
1.0
|
C
|
A:HIS96
|
4.6
|
9.0
|
1.0
|
N
|
A:HIS96
|
4.8
|
9.1
|
1.0
|
O
|
A:LEU95
|
5.0
|
8.2
|
1.0
|
|
Copper binding site 5 out
of 8 in 6i3k
Go back to
Copper Binding Sites List in 6i3k
Copper binding site 5 out
of 8 in the Bilirubin Oxidase From Myrothecium Verrucaria, Mutant W396A in Complex with Ferricyanide
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 5 of Bilirubin Oxidase From Myrothecium Verrucaria, Mutant W396A in Complex with Ferricyanide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu601
b:12.7
occ:1.00
|
ND1
|
B:HIS398
|
2.0
|
12.4
|
1.0
|
ND1
|
B:HIS462
|
2.1
|
13.0
|
1.0
|
SG
|
B:CYS457
|
2.2
|
11.8
|
1.0
|
CE1
|
B:HIS398
|
3.0
|
13.7
|
1.0
|
CE1
|
B:HIS462
|
3.0
|
12.1
|
1.0
|
CG
|
B:HIS398
|
3.0
|
11.8
|
1.0
|
CG
|
B:HIS462
|
3.1
|
12.2
|
1.0
|
CB
|
B:CYS457
|
3.2
|
11.6
|
1.0
|
CB
|
B:HIS462
|
3.3
|
12.1
|
1.0
|
CB
|
B:HIS398
|
3.4
|
11.7
|
1.0
|
SD
|
B:MET467
|
3.4
|
14.6
|
1.0
|
O
|
B:THR397
|
3.4
|
11.5
|
1.0
|
CA
|
B:HIS398
|
3.6
|
10.5
|
1.0
|
CB
|
B:ASN459
|
4.0
|
10.8
|
1.0
|
NE2
|
B:HIS398
|
4.1
|
14.0
|
1.0
|
CD2
|
B:HIS398
|
4.2
|
13.8
|
1.0
|
NE2
|
B:HIS462
|
4.2
|
13.1
|
1.0
|
CD2
|
B:HIS462
|
4.2
|
12.5
|
1.0
|
C
|
B:THR397
|
4.2
|
11.9
|
1.0
|
N
|
B:HIS398
|
4.3
|
11.9
|
1.0
|
CE
|
B:MET467
|
4.4
|
13.9
|
1.0
|
CA
|
B:CYS457
|
4.6
|
11.2
|
1.0
|
C
|
B:HIS398
|
4.8
|
10.7
|
1.0
|
CD
|
B:PRO399
|
4.8
|
11.4
|
1.0
|
CG
|
B:ASN459
|
4.8
|
11.0
|
1.0
|
CA
|
B:HIS462
|
4.8
|
12.5
|
1.0
|
N
|
B:ASN459
|
4.9
|
10.8
|
1.0
|
CG
|
B:MET467
|
4.9
|
13.5
|
1.0
|
ND2
|
B:ASN459
|
5.0
|
10.8
|
1.0
|
|
Copper binding site 6 out
of 8 in 6i3k
Go back to
Copper Binding Sites List in 6i3k
Copper binding site 6 out
of 8 in the Bilirubin Oxidase From Myrothecium Verrucaria, Mutant W396A in Complex with Ferricyanide
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 6 of Bilirubin Oxidase From Myrothecium Verrucaria, Mutant W396A in Complex with Ferricyanide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu602
b:13.0
occ:1.00
|
NE2
|
B:HIS456
|
2.0
|
10.9
|
1.0
|
NE2
|
B:HIS403
|
2.0
|
10.9
|
1.0
|
NE2
|
B:HIS136
|
2.0
|
12.4
|
1.0
|
O
|
B:HOH1145
|
2.3
|
26.4
|
0.5
|
CD2
|
B:HIS456
|
2.9
|
12.3
|
1.0
|
CE1
|
B:HIS403
|
3.0
|
11.6
|
1.0
|
CE1
|
B:HIS136
|
3.0
|
12.8
|
1.0
|
CE1
|
B:HIS456
|
3.0
|
11.7
|
1.0
|
CD2
|
B:HIS136
|
3.1
|
13.2
|
1.0
|
CD2
|
B:HIS403
|
3.1
|
11.3
|
1.0
|
CD2
|
B:HIS401
|
3.8
|
10.8
|
1.0
|
CE
|
B:MET454
|
3.9
|
13.0
|
1.0
|
CG
|
B:HIS456
|
4.0
|
11.5
|
1.0
|
ND1
|
B:HIS456
|
4.1
|
11.3
|
1.0
|
ND1
|
B:HIS403
|
4.1
|
10.5
|
1.0
|
ND1
|
B:HIS136
|
4.1
|
11.9
|
1.0
|
CG
|
B:HIS136
|
4.2
|
12.3
|
1.0
|
CG
|
B:HIS403
|
4.2
|
10.9
|
1.0
|
CD2
|
B:HIS94
|
4.3
|
11.0
|
1.0
|
CU
|
B:CU604
|
4.3
|
13.7
|
1.0
|
NE2
|
B:HIS401
|
4.4
|
10.5
|
1.0
|
NE2
|
B:HIS94
|
4.5
|
10.5
|
1.0
|
CB
|
B:MET454
|
4.6
|
12.1
|
1.0
|
SD
|
B:MET454
|
4.8
|
14.4
|
1.0
|
OE2
|
B:GLU463
|
4.8
|
15.1
|
1.0
|
CG
|
B:HIS94
|
4.9
|
10.4
|
1.0
|
CG
|
B:HIS401
|
4.9
|
10.8
|
1.0
|
CD2
|
B:HIS458
|
5.0
|
12.1
|
1.0
|
NE2
|
B:HIS458
|
5.0
|
11.4
|
1.0
|
CU
|
B:CU603
|
5.0
|
12.6
|
1.0
|
|
Copper binding site 7 out
of 8 in 6i3k
Go back to
Copper Binding Sites List in 6i3k
Copper binding site 7 out
of 8 in the Bilirubin Oxidase From Myrothecium Verrucaria, Mutant W396A in Complex with Ferricyanide
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 7 of Bilirubin Oxidase From Myrothecium Verrucaria, Mutant W396A in Complex with Ferricyanide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu603
b:12.6
occ:1.00
|
NE2
|
B:HIS134
|
2.0
|
11.8
|
1.0
|
ND1
|
B:HIS96
|
2.0
|
10.0
|
1.0
|
NE2
|
B:HIS458
|
2.1
|
11.4
|
1.0
|
O
|
B:HOH1145
|
2.7
|
26.4
|
0.5
|
CE1
|
B:HIS96
|
2.9
|
9.9
|
1.0
|
CE1
|
B:HIS134
|
2.9
|
13.2
|
1.0
|
CD2
|
B:HIS134
|
3.0
|
11.5
|
1.0
|
CE1
|
B:HIS458
|
3.1
|
11.4
|
1.0
|
CG
|
B:HIS96
|
3.1
|
10.5
|
1.0
|
CD2
|
B:HIS458
|
3.2
|
12.1
|
1.0
|
CB
|
B:HIS96
|
3.5
|
10.6
|
1.0
|
CZ2
|
B:TRP132
|
3.6
|
13.0
|
1.0
|
CD2
|
B:HIS94
|
3.9
|
11.0
|
1.0
|
CE2
|
B:TRP132
|
3.9
|
12.5
|
1.0
|
NE1
|
B:TRP132
|
4.0
|
12.1
|
1.0
|
ND1
|
B:HIS134
|
4.1
|
12.5
|
1.0
|
NE2
|
B:HIS96
|
4.1
|
9.9
|
1.0
|
CG
|
B:HIS134
|
4.1
|
11.7
|
1.0
|
CD2
|
B:HIS96
|
4.2
|
9.8
|
1.0
|
ND1
|
B:HIS458
|
4.2
|
11.4
|
1.0
|
CB
|
B:ALA274
|
4.2
|
10.7
|
1.0
|
CU
|
B:CU604
|
4.3
|
13.7
|
1.0
|
CG
|
B:HIS458
|
4.3
|
11.0
|
1.0
|
CH2
|
B:TRP132
|
4.4
|
13.1
|
1.0
|
NE2
|
B:HIS94
|
4.4
|
10.5
|
1.0
|
CD2
|
B:HIS401
|
4.4
|
10.8
|
1.0
|
NE2
|
B:HIS401
|
4.6
|
10.5
|
1.0
|
CA
|
B:HIS96
|
4.8
|
10.0
|
1.0
|
CD2
|
B:TRP132
|
4.9
|
13.0
|
1.0
|
CU
|
B:CU602
|
5.0
|
13.0
|
1.0
|
CD1
|
B:TRP132
|
5.0
|
13.0
|
1.0
|
|
Copper binding site 8 out
of 8 in 6i3k
Go back to
Copper Binding Sites List in 6i3k
Copper binding site 8 out
of 8 in the Bilirubin Oxidase From Myrothecium Verrucaria, Mutant W396A in Complex with Ferricyanide
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 8 of Bilirubin Oxidase From Myrothecium Verrucaria, Mutant W396A in Complex with Ferricyanide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu604
b:13.7
occ:1.00
|
NE2
|
B:HIS401
|
1.9
|
10.5
|
1.0
|
NE2
|
B:HIS94
|
1.9
|
10.5
|
1.0
|
O
|
B:HOH1163
|
2.6
|
12.1
|
1.0
|
CE1
|
B:HIS94
|
2.8
|
10.5
|
1.0
|
CD2
|
B:HIS401
|
2.8
|
10.8
|
1.0
|
CE1
|
B:HIS401
|
2.9
|
10.9
|
1.0
|
CD2
|
B:HIS94
|
2.9
|
11.0
|
1.0
|
NE2
|
B:HIS403
|
3.3
|
10.9
|
1.0
|
CG
|
B:HIS96
|
3.4
|
10.5
|
1.0
|
ND1
|
B:HIS96
|
3.4
|
10.0
|
1.0
|
CD2
|
B:HIS403
|
3.5
|
11.3
|
1.0
|
CE1
|
B:HIS403
|
3.5
|
11.6
|
1.0
|
O
|
B:HOH1145
|
3.7
|
26.4
|
0.5
|
CD2
|
B:HIS96
|
3.7
|
9.8
|
1.0
|
CA
|
B:HIS96
|
3.8
|
10.0
|
1.0
|
CE1
|
B:HIS96
|
3.8
|
9.9
|
1.0
|
ND1
|
B:HIS403
|
3.8
|
10.5
|
1.0
|
CG
|
B:HIS403
|
3.8
|
10.9
|
1.0
|
CB
|
B:HIS96
|
3.9
|
10.6
|
1.0
|
ND1
|
B:HIS94
|
3.9
|
10.3
|
1.0
|
ND1
|
B:HIS401
|
4.0
|
10.4
|
1.0
|
NE2
|
B:HIS96
|
4.0
|
9.9
|
1.0
|
CG
|
B:HIS401
|
4.0
|
10.8
|
1.0
|
CG
|
B:HIS94
|
4.0
|
10.4
|
1.0
|
CU
|
B:CU602
|
4.3
|
13.0
|
1.0
|
CU
|
B:CU603
|
4.3
|
12.6
|
1.0
|
N
|
B:GLY97
|
4.4
|
10.2
|
1.0
|
O
|
B:HOH980
|
4.5
|
10.5
|
1.0
|
O
|
B:HOH1023
|
4.6
|
11.0
|
1.0
|
C
|
B:HIS96
|
4.6
|
10.9
|
1.0
|
CA
|
B:HIS403
|
4.6
|
11.1
|
1.0
|
CB
|
B:HIS403
|
4.7
|
11.0
|
1.0
|
N
|
B:HIS96
|
4.8
|
9.8
|
1.0
|
|
Reference:
T.Koval,
L.Svecova,
L.H.Ostergaard,
T.Skalova,
J.Duskova,
J.Hasek,
P.Kolenko,
K.Fejfarova,
J.Stransky,
M.Trundova,
J.Dohnalek.
Trp-His Covalent Adduct in Bilirubin Oxidase Is Crucial For Effective Bilirubin Binding But Has A Minor Role in Electron Transfer. Sci Rep V. 9 13700 2019.
ISSN: ESSN 2045-2322
PubMed: 31548583
DOI: 10.1038/S41598-019-50105-3
Page generated: Wed Jul 31 06:12:15 2024
|