Iron in PDB 7oih: Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase
Enzymatic activity of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase
All present enzymatic activity of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase:
1.11.2.2;
Protein crystallography data
The structure of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase, PDB code: 7oih
was solved by
L.Krawczyk,
S.Semwal,
J.Bouckaert,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
38.99 /
2.60
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
155.91,
144.634,
236.454,
90,
91.53,
90
|
R / Rfree (%)
|
17.9 /
22
|
Other elements in 7oih:
The structure of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase
(pdb code 7oih). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 8 binding sites of Iron where determined in the
Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase, PDB code: 7oih:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Iron binding site 1 out
of 8 in 7oih
Go back to
Iron Binding Sites List in 7oih
Iron binding site 1 out
of 8 in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe805
b:46.1
occ:1.00
|
FE
|
A:HEM805
|
0.0
|
46.1
|
1.0
|
ND
|
A:HEM805
|
1.9
|
52.3
|
1.0
|
NA
|
A:HEM805
|
2.0
|
50.1
|
1.0
|
NE2
|
A:HIS502
|
2.1
|
44.0
|
1.0
|
O
|
A:HOH905
|
2.1
|
48.4
|
1.0
|
NC
|
A:HEM805
|
2.1
|
48.5
|
1.0
|
NB
|
A:HEM805
|
2.1
|
54.5
|
1.0
|
C4D
|
A:HEM805
|
2.9
|
50.5
|
1.0
|
C1D
|
A:HEM805
|
3.0
|
43.0
|
1.0
|
C1A
|
A:HEM805
|
3.0
|
51.3
|
1.0
|
C4A
|
A:HEM805
|
3.0
|
51.2
|
1.0
|
C4C
|
A:HEM805
|
3.1
|
43.0
|
1.0
|
C1B
|
A:HEM805
|
3.1
|
51.1
|
1.0
|
CD2
|
A:HIS502
|
3.1
|
40.8
|
1.0
|
CE1
|
A:HIS502
|
3.1
|
36.8
|
1.0
|
C1C
|
A:HEM805
|
3.2
|
50.0
|
1.0
|
C4B
|
A:HEM805
|
3.2
|
54.8
|
1.0
|
CHA
|
A:HEM805
|
3.3
|
52.4
|
1.0
|
CHD
|
A:HEM805
|
3.4
|
41.6
|
1.0
|
CHB
|
A:HEM805
|
3.4
|
51.5
|
1.0
|
CHC
|
A:HEM805
|
3.5
|
50.6
|
1.0
|
C3A
|
A:HEM805
|
4.2
|
53.3
|
1.0
|
C2A
|
A:HEM805
|
4.2
|
49.5
|
1.0
|
C2D
|
A:HEM805
|
4.2
|
40.1
|
1.0
|
C3D
|
A:HEM805
|
4.2
|
43.0
|
1.0
|
CG
|
A:HIS502
|
4.2
|
35.0
|
1.0
|
ND1
|
A:HIS502
|
4.2
|
31.6
|
1.0
|
C3C
|
A:HEM805
|
4.3
|
44.5
|
1.0
|
C2C
|
A:HEM805
|
4.3
|
45.0
|
1.0
|
C2B
|
A:HEM805
|
4.3
|
53.5
|
1.0
|
C3B
|
A:HEM805
|
4.4
|
57.8
|
1.0
|
CD2
|
A:LEU583
|
4.5
|
38.6
|
1.0
|
N
|
A:SCN806
|
4.7
|
77.1
|
1.0
|
|
Iron binding site 2 out
of 8 in 7oih
Go back to
Iron Binding Sites List in 7oih
Iron binding site 2 out
of 8 in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe807
b:51.6
occ:1.00
|
FE
|
B:HEM807
|
0.0
|
51.6
|
1.0
|
ND
|
B:HEM807
|
1.9
|
54.0
|
1.0
|
NE2
|
B:HIS502
|
2.0
|
51.1
|
1.0
|
O
|
B:HOH912
|
2.0
|
67.0
|
1.0
|
NA
|
B:HEM807
|
2.1
|
53.6
|
1.0
|
NB
|
B:HEM807
|
2.1
|
48.3
|
1.0
|
NC
|
B:HEM807
|
2.1
|
48.1
|
1.0
|
C1D
|
B:HEM807
|
2.9
|
51.5
|
1.0
|
C4D
|
B:HEM807
|
2.9
|
47.0
|
1.0
|
CD2
|
B:HIS502
|
3.0
|
50.6
|
1.0
|
CE1
|
B:HIS502
|
3.0
|
48.9
|
1.0
|
C1B
|
B:HEM807
|
3.1
|
42.7
|
1.0
|
C4B
|
B:HEM807
|
3.1
|
51.2
|
1.0
|
C1A
|
B:HEM807
|
3.1
|
48.2
|
1.0
|
C4C
|
B:HEM807
|
3.1
|
46.3
|
1.0
|
C4A
|
B:HEM807
|
3.1
|
47.7
|
1.0
|
C1C
|
B:HEM807
|
3.2
|
45.7
|
1.0
|
CHA
|
B:HEM807
|
3.4
|
48.7
|
1.0
|
CHD
|
B:HEM807
|
3.4
|
43.2
|
1.0
|
CHB
|
B:HEM807
|
3.5
|
43.6
|
1.0
|
CHC
|
B:HEM807
|
3.5
|
43.1
|
1.0
|
ND1
|
B:HIS502
|
4.2
|
42.6
|
1.0
|
C2D
|
B:HEM807
|
4.2
|
48.1
|
1.0
|
CG
|
B:HIS502
|
4.2
|
45.7
|
1.0
|
C3D
|
B:HEM807
|
4.2
|
44.3
|
1.0
|
C3B
|
B:HEM807
|
4.3
|
49.9
|
1.0
|
C2A
|
B:HEM807
|
4.3
|
42.4
|
1.0
|
C2B
|
B:HEM807
|
4.3
|
49.1
|
1.0
|
C3C
|
B:HEM807
|
4.3
|
44.5
|
1.0
|
C3A
|
B:HEM807
|
4.3
|
45.0
|
1.0
|
C2C
|
B:HEM807
|
4.4
|
43.6
|
1.0
|
CD2
|
B:LEU583
|
4.6
|
40.4
|
1.0
|
N
|
B:SCN808
|
4.8
|
62.9
|
1.0
|
|
Iron binding site 3 out
of 8 in 7oih
Go back to
Iron Binding Sites List in 7oih
Iron binding site 3 out
of 8 in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe806
b:54.2
occ:1.00
|
FE
|
C:HEM806
|
0.0
|
54.2
|
1.0
|
ND
|
C:HEM806
|
2.0
|
59.1
|
1.0
|
O
|
C:HOH906
|
2.0
|
62.2
|
1.0
|
NA
|
C:HEM806
|
2.0
|
51.3
|
1.0
|
NE2
|
C:HIS502
|
2.1
|
52.1
|
1.0
|
NC
|
C:HEM806
|
2.1
|
51.2
|
1.0
|
NB
|
C:HEM806
|
2.1
|
51.2
|
1.0
|
C1D
|
C:HEM806
|
3.0
|
50.6
|
1.0
|
C4D
|
C:HEM806
|
3.0
|
48.6
|
1.0
|
C4C
|
C:HEM806
|
3.0
|
52.3
|
1.0
|
C1B
|
C:HEM806
|
3.0
|
48.9
|
1.0
|
C1A
|
C:HEM806
|
3.1
|
49.7
|
1.0
|
C4A
|
C:HEM806
|
3.1
|
54.2
|
1.0
|
CD2
|
C:HIS502
|
3.1
|
50.2
|
1.0
|
CE1
|
C:HIS502
|
3.1
|
52.8
|
1.0
|
C4B
|
C:HEM806
|
3.1
|
51.1
|
1.0
|
C1C
|
C:HEM806
|
3.2
|
50.2
|
1.0
|
CHD
|
C:HEM806
|
3.4
|
51.2
|
1.0
|
CHA
|
C:HEM806
|
3.4
|
46.9
|
1.0
|
CHB
|
C:HEM806
|
3.4
|
49.4
|
1.0
|
CHC
|
C:HEM806
|
3.5
|
46.8
|
1.0
|
ND1
|
C:HIS502
|
4.2
|
43.0
|
1.0
|
C2D
|
C:HEM806
|
4.2
|
47.5
|
1.0
|
C3C
|
C:HEM806
|
4.2
|
45.6
|
1.0
|
CG
|
C:HIS502
|
4.2
|
45.7
|
1.0
|
C3D
|
C:HEM806
|
4.3
|
49.8
|
1.0
|
C3A
|
C:HEM806
|
4.3
|
53.8
|
1.0
|
C2C
|
C:HEM806
|
4.3
|
44.5
|
1.0
|
C2B
|
C:HEM806
|
4.3
|
53.3
|
1.0
|
C2A
|
C:HEM806
|
4.3
|
48.3
|
1.0
|
C3B
|
C:HEM806
|
4.3
|
52.6
|
1.0
|
CD2
|
C:LEU583
|
4.6
|
47.9
|
1.0
|
N
|
C:SCN807
|
4.6
|
75.6
|
1.0
|
|
Iron binding site 4 out
of 8 in 7oih
Go back to
Iron Binding Sites List in 7oih
Iron binding site 4 out
of 8 in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe805
b:53.2
occ:1.00
|
FE
|
D:HEM805
|
0.0
|
53.2
|
1.0
|
ND
|
D:HEM805
|
1.9
|
51.0
|
1.0
|
NA
|
D:HEM805
|
2.1
|
53.0
|
1.0
|
O
|
D:HOH904
|
2.1
|
55.1
|
1.0
|
NC
|
D:HEM805
|
2.1
|
43.5
|
1.0
|
NB
|
D:HEM805
|
2.1
|
54.1
|
1.0
|
NE2
|
D:HIS502
|
2.1
|
47.3
|
1.0
|
C1D
|
D:HEM805
|
2.9
|
45.3
|
1.0
|
C4D
|
D:HEM805
|
2.9
|
48.1
|
1.0
|
C4C
|
D:HEM805
|
3.0
|
38.5
|
1.0
|
C1A
|
D:HEM805
|
3.0
|
52.0
|
1.0
|
C4B
|
D:HEM805
|
3.0
|
52.8
|
1.0
|
C1C
|
D:HEM805
|
3.1
|
45.0
|
1.0
|
C1B
|
D:HEM805
|
3.1
|
51.7
|
1.0
|
C4A
|
D:HEM805
|
3.1
|
50.2
|
1.0
|
CE1
|
D:HIS502
|
3.1
|
46.3
|
1.0
|
CD2
|
D:HIS502
|
3.2
|
47.0
|
1.0
|
CHD
|
D:HEM805
|
3.3
|
40.6
|
1.0
|
CHA
|
D:HEM805
|
3.4
|
53.8
|
1.0
|
CHC
|
D:HEM805
|
3.4
|
47.8
|
1.0
|
CHB
|
D:HEM805
|
3.5
|
49.4
|
1.0
|
C2D
|
D:HEM805
|
4.2
|
45.8
|
1.0
|
C3C
|
D:HEM805
|
4.2
|
41.1
|
1.0
|
C3D
|
D:HEM805
|
4.2
|
46.0
|
1.0
|
C2C
|
D:HEM805
|
4.2
|
43.2
|
1.0
|
C2A
|
D:HEM805
|
4.3
|
46.4
|
1.0
|
N
|
D:SCN806
|
4.3
|
53.1
|
1.0
|
C3A
|
D:HEM805
|
4.3
|
52.9
|
1.0
|
ND1
|
D:HIS502
|
4.3
|
37.8
|
1.0
|
C3B
|
D:HEM805
|
4.3
|
56.2
|
1.0
|
CG
|
D:HIS502
|
4.3
|
38.8
|
1.0
|
C2B
|
D:HEM805
|
4.3
|
56.1
|
1.0
|
CD2
|
D:LEU583
|
4.6
|
39.6
|
1.0
|
O
|
D:HOH944
|
5.0
|
49.8
|
1.0
|
|
Iron binding site 5 out
of 8 in 7oih
Go back to
Iron Binding Sites List in 7oih
Iron binding site 5 out
of 8 in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Fe805
b:55.5
occ:1.00
|
FE
|
E:HEM805
|
0.0
|
55.5
|
1.0
|
ND
|
E:HEM805
|
1.9
|
64.2
|
1.0
|
NA
|
E:HEM805
|
2.0
|
52.5
|
1.0
|
O
|
E:HOH927
|
2.1
|
64.1
|
1.0
|
NE2
|
E:HIS502
|
2.1
|
56.5
|
1.0
|
NC
|
E:HEM805
|
2.1
|
54.8
|
1.0
|
NB
|
E:HEM805
|
2.1
|
54.9
|
1.0
|
C4D
|
E:HEM805
|
2.9
|
60.4
|
1.0
|
C1D
|
E:HEM805
|
3.0
|
52.7
|
1.0
|
C1A
|
E:HEM805
|
3.0
|
51.3
|
1.0
|
C4C
|
E:HEM805
|
3.1
|
53.1
|
1.0
|
C4A
|
E:HEM805
|
3.1
|
51.3
|
1.0
|
C1B
|
E:HEM805
|
3.1
|
53.4
|
1.0
|
CD2
|
E:HIS502
|
3.1
|
54.7
|
1.0
|
C1C
|
E:HEM805
|
3.1
|
54.0
|
1.0
|
C4B
|
E:HEM805
|
3.1
|
52.5
|
1.0
|
CE1
|
E:HIS502
|
3.1
|
55.9
|
1.0
|
CHA
|
E:HEM805
|
3.3
|
52.5
|
1.0
|
CHD
|
E:HEM805
|
3.4
|
50.9
|
1.0
|
CHB
|
E:HEM805
|
3.5
|
55.5
|
1.0
|
CHC
|
E:HEM805
|
3.5
|
52.0
|
1.0
|
C3D
|
E:HEM805
|
4.2
|
56.7
|
1.0
|
C2D
|
E:HEM805
|
4.2
|
52.7
|
1.0
|
C2A
|
E:HEM805
|
4.2
|
55.6
|
1.0
|
ND1
|
E:HIS502
|
4.2
|
51.5
|
1.0
|
C3A
|
E:HEM805
|
4.2
|
52.2
|
1.0
|
CG
|
E:HIS502
|
4.3
|
53.5
|
1.0
|
C2C
|
E:HEM805
|
4.3
|
56.7
|
1.0
|
C3C
|
E:HEM805
|
4.3
|
56.0
|
1.0
|
C2B
|
E:HEM805
|
4.3
|
54.1
|
1.0
|
C3B
|
E:HEM805
|
4.4
|
52.4
|
1.0
|
CD2
|
E:LEU583
|
4.6
|
53.0
|
1.0
|
N
|
E:SCN806
|
4.9
|
64.8
|
1.0
|
|
Iron binding site 6 out
of 8 in 7oih
Go back to
Iron Binding Sites List in 7oih
Iron binding site 6 out
of 8 in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 6 of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Fe805
b:58.0
occ:1.00
|
FE
|
F:HEM805
|
0.0
|
58.0
|
1.0
|
ND
|
F:HEM805
|
1.9
|
57.0
|
1.0
|
NA
|
F:HEM805
|
2.0
|
64.3
|
1.0
|
O
|
F:HOH905
|
2.0
|
54.3
|
1.0
|
NE2
|
F:HIS502
|
2.1
|
50.3
|
1.0
|
NB
|
F:HEM805
|
2.1
|
61.0
|
1.0
|
NC
|
F:HEM805
|
2.2
|
57.8
|
1.0
|
C4D
|
F:HEM805
|
2.9
|
49.5
|
1.0
|
C1D
|
F:HEM805
|
3.0
|
53.5
|
1.0
|
C1A
|
F:HEM805
|
3.0
|
54.8
|
1.0
|
CD2
|
F:HIS502
|
3.1
|
49.4
|
1.0
|
C4B
|
F:HEM805
|
3.1
|
60.0
|
1.0
|
C1B
|
F:HEM805
|
3.1
|
60.5
|
1.0
|
C4A
|
F:HEM805
|
3.1
|
64.0
|
1.0
|
CE1
|
F:HIS502
|
3.1
|
51.2
|
1.0
|
C4C
|
F:HEM805
|
3.1
|
51.4
|
1.0
|
C1C
|
F:HEM805
|
3.2
|
57.9
|
1.0
|
CHA
|
F:HEM805
|
3.3
|
56.6
|
1.0
|
CHD
|
F:HEM805
|
3.4
|
53.5
|
1.0
|
CHB
|
F:HEM805
|
3.5
|
61.9
|
1.0
|
CHC
|
F:HEM805
|
3.5
|
56.0
|
1.0
|
C3D
|
F:HEM805
|
4.2
|
46.1
|
1.0
|
C2D
|
F:HEM805
|
4.2
|
44.9
|
1.0
|
CG
|
F:HIS502
|
4.2
|
44.0
|
1.0
|
ND1
|
F:HIS502
|
4.2
|
38.2
|
1.0
|
C2A
|
F:HEM805
|
4.2
|
50.2
|
1.0
|
C3A
|
F:HEM805
|
4.3
|
56.3
|
1.0
|
C2B
|
F:HEM805
|
4.3
|
58.6
|
1.0
|
C3B
|
F:HEM805
|
4.3
|
58.8
|
1.0
|
C3C
|
F:HEM805
|
4.3
|
52.5
|
1.0
|
C2C
|
F:HEM805
|
4.3
|
58.9
|
1.0
|
CD2
|
F:LEU583
|
4.6
|
40.8
|
1.0
|
N
|
F:SCN806
|
4.8
|
71.2
|
1.0
|
|
Iron binding site 7 out
of 8 in 7oih
Go back to
Iron Binding Sites List in 7oih
Iron binding site 7 out
of 8 in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 7 of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Fe806
b:42.3
occ:1.00
|
FE
|
G:HEM806
|
0.0
|
42.3
|
1.0
|
ND
|
G:HEM806
|
1.9
|
43.5
|
1.0
|
NA
|
G:HEM806
|
2.0
|
39.3
|
1.0
|
NC
|
G:HEM806
|
2.1
|
35.7
|
1.0
|
O
|
G:HOH917
|
2.1
|
54.5
|
1.0
|
NE2
|
G:HIS502
|
2.1
|
42.0
|
1.0
|
NB
|
G:HEM806
|
2.1
|
39.9
|
1.0
|
C1D
|
G:HEM806
|
2.9
|
40.6
|
1.0
|
C4D
|
G:HEM806
|
3.0
|
38.1
|
1.0
|
C4C
|
G:HEM806
|
3.0
|
35.2
|
1.0
|
C1A
|
G:HEM806
|
3.0
|
35.8
|
1.0
|
C1B
|
G:HEM806
|
3.1
|
39.2
|
1.0
|
C1C
|
G:HEM806
|
3.1
|
35.1
|
1.0
|
C4A
|
G:HEM806
|
3.1
|
40.2
|
1.0
|
CE1
|
G:HIS502
|
3.1
|
42.3
|
1.0
|
C4B
|
G:HEM806
|
3.1
|
39.6
|
1.0
|
CD2
|
G:HIS502
|
3.1
|
44.4
|
1.0
|
CHA
|
G:HEM806
|
3.4
|
37.4
|
1.0
|
CHD
|
G:HEM806
|
3.4
|
37.6
|
1.0
|
CHB
|
G:HEM806
|
3.5
|
38.6
|
1.0
|
CHC
|
G:HEM806
|
3.5
|
32.9
|
1.0
|
C3C
|
G:HEM806
|
4.2
|
36.1
|
1.0
|
C2D
|
G:HEM806
|
4.2
|
41.9
|
1.0
|
C2C
|
G:HEM806
|
4.2
|
39.0
|
1.0
|
C3D
|
G:HEM806
|
4.2
|
40.7
|
1.0
|
C2A
|
G:HEM806
|
4.2
|
37.9
|
1.0
|
ND1
|
G:HIS502
|
4.2
|
40.2
|
1.0
|
C3A
|
G:HEM806
|
4.3
|
38.4
|
1.0
|
CG
|
G:HIS502
|
4.3
|
41.8
|
1.0
|
C2B
|
G:HEM806
|
4.3
|
43.9
|
1.0
|
C3B
|
G:HEM806
|
4.4
|
44.4
|
1.0
|
CD2
|
G:LEU583
|
4.6
|
37.5
|
1.0
|
O
|
G:HOH960
|
4.7
|
44.5
|
1.0
|
|
Iron binding site 8 out
of 8 in 7oih
Go back to
Iron Binding Sites List in 7oih
Iron binding site 8 out
of 8 in the Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 8 of Glycosylation in the Crystal Structure of Neutrophil Myeloperoxidase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Fe805
b:58.6
occ:1.00
|
FE
|
H:HEM805
|
0.0
|
58.6
|
1.0
|
ND
|
H:HEM805
|
1.9
|
58.0
|
1.0
|
NA
|
H:HEM805
|
2.0
|
57.9
|
1.0
|
O
|
H:HOH906
|
2.0
|
50.2
|
1.0
|
NE2
|
H:HIS502
|
2.1
|
51.0
|
1.0
|
NB
|
H:HEM805
|
2.1
|
57.1
|
1.0
|
NC
|
H:HEM805
|
2.1
|
55.5
|
1.0
|
C1D
|
H:HEM805
|
3.0
|
50.1
|
1.0
|
C4D
|
H:HEM805
|
3.0
|
54.6
|
1.0
|
C1A
|
H:HEM805
|
3.0
|
57.6
|
1.0
|
C4A
|
H:HEM805
|
3.1
|
56.3
|
1.0
|
C1B
|
H:HEM805
|
3.1
|
56.5
|
1.0
|
C4C
|
H:HEM805
|
3.1
|
51.1
|
1.0
|
CD2
|
H:HIS502
|
3.1
|
44.3
|
1.0
|
C4B
|
H:HEM805
|
3.1
|
57.9
|
1.0
|
CE1
|
H:HIS502
|
3.1
|
52.8
|
1.0
|
C1C
|
H:HEM805
|
3.2
|
59.3
|
1.0
|
CHA
|
H:HEM805
|
3.4
|
56.9
|
1.0
|
CHD
|
H:HEM805
|
3.4
|
51.9
|
1.0
|
CHB
|
H:HEM805
|
3.5
|
59.3
|
1.0
|
CHC
|
H:HEM805
|
3.5
|
54.7
|
1.0
|
C2D
|
H:HEM805
|
4.2
|
49.0
|
1.0
|
C3A
|
H:HEM805
|
4.2
|
49.2
|
1.0
|
C2A
|
H:HEM805
|
4.2
|
50.6
|
1.0
|
ND1
|
H:HIS502
|
4.2
|
42.4
|
1.0
|
CG
|
H:HIS502
|
4.2
|
42.4
|
1.0
|
C3D
|
H:HEM805
|
4.2
|
53.7
|
1.0
|
C3C
|
H:HEM805
|
4.3
|
52.4
|
1.0
|
C2B
|
H:HEM805
|
4.3
|
53.7
|
1.0
|
C2C
|
H:HEM805
|
4.3
|
58.1
|
1.0
|
C3B
|
H:HEM805
|
4.3
|
60.2
|
1.0
|
CD2
|
H:LEU583
|
4.6
|
39.8
|
1.0
|
N
|
H:SCN806
|
5.0
|
60.7
|
1.0
|
|
Reference:
L.Krawczyk,
S.Semwal,
J.Soubhye,
S.Lemri Ouadriri,
M.Prevost,
P.Van Antwerpen,
G.Roos,
J.Bouckaert.
Native Glycosylation and Binding of the Antidepressant Paroxetine in A Low-Resolution Crystal Structure of Human Myeloperoxidase. Acta Crystallogr D Struct V. 78 1099 2022BIOL.
ISSN: ISSN 2059-7983
PubMed: 36048150
DOI: 10.1107/S2059798322007082
Page generated: Thu Aug 8 14:23:41 2024
|