Manganese in PDB 6yvt: Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Md-253
Enzymatic activity of Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Md-253
All present enzymatic activity of Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Md-253:
1.14.11.29;
Protein crystallography data
The structure of Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Md-253, PDB code: 6yvt
was solved by
R.Chowdhury,
M.Demetriades,
C.J.Schofield,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
23.75 /
2.85
|
|
Space group
|
P 21 21 21
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
84.456,
103.018,
196.028,
90.00,
90.00,
90.00
|
|
R / Rfree (%)
|
23.7 /
26.6
|
Manganese Binding Sites:
The binding sites of Manganese atom in the Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Md-253
(pdb code 6yvt). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 6 binding sites of Manganese where determined in the
Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Md-253, PDB code: 6yvt:
Jump to Manganese binding site number:
1;
2;
3;
4;
5;
6;
Manganese binding site 1 out
of 6 in 6yvt
Go back to
Manganese Binding Sites List in 6yvt
Manganese binding site 1 out
of 6 in the Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Md-253
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Md-253 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn501
b:36.4
occ:1.00
|
O26
|
A:PW2502
|
2.0
|
31.6
|
1.0
|
|
N18
|
A:PW2502
|
2.1
|
41.4
|
1.0
|
|
NE2
|
A:HIS313
|
2.1
|
37.0
|
1.0
|
|
OD1
|
A:ASP315
|
2.3
|
49.8
|
1.0
|
|
C20
|
A:PW2502
|
2.5
|
33.3
|
1.0
|
|
NE2
|
A:HIS374
|
2.5
|
31.8
|
1.0
|
|
C19
|
A:PW2502
|
2.6
|
40.0
|
1.0
|
|
O
|
A:HOH605
|
2.8
|
25.4
|
1.0
|
|
CE1
|
A:HIS313
|
2.9
|
38.3
|
1.0
|
|
HE1
|
A:HIS313
|
2.9
|
46.0
|
1.0
|
|
C17
|
A:PW2502
|
3.2
|
40.8
|
1.0
|
|
CG
|
A:ASP315
|
3.2
|
49.1
|
1.0
|
|
CD2
|
A:HIS313
|
3.3
|
40.5
|
1.0
|
|
H171
|
A:PW2502
|
3.4
|
49.0
|
1.0
|
|
CD2
|
A:HIS374
|
3.4
|
26.5
|
1.0
|
|
OD2
|
A:ASP315
|
3.4
|
49.0
|
1.0
|
|
HD2
|
A:HIS374
|
3.5
|
31.9
|
1.0
|
|
CE1
|
A:HIS374
|
3.6
|
32.6
|
1.0
|
|
HD2
|
A:HIS313
|
3.6
|
48.6
|
1.0
|
|
HE1
|
A:HIS374
|
3.7
|
39.2
|
1.0
|
|
N21
|
A:PW2502
|
3.9
|
33.7
|
1.0
|
|
C02
|
A:PW2502
|
4.0
|
38.4
|
1.0
|
|
HZ
|
A:PHE366
|
4.0
|
40.3
|
1.0
|
|
ND1
|
A:HIS313
|
4.1
|
34.7
|
1.0
|
|
HZ2
|
A:TRP389
|
4.1
|
48.9
|
1.0
|
|
CG
|
A:HIS313
|
4.3
|
40.1
|
1.0
|
|
HG11
|
C:VAL401
|
4.3
|
71.1
|
1.0
|
|
C04
|
A:PW2502
|
4.4
|
37.0
|
1.0
|
|
H211
|
A:PW2502
|
4.4
|
40.5
|
1.0
|
|
H222
|
A:PW2502
|
4.5
|
37.9
|
1.0
|
|
HA
|
A:ASP315
|
4.5
|
65.9
|
1.0
|
|
CG
|
A:HIS374
|
4.6
|
32.4
|
1.0
|
|
ND1
|
A:HIS374
|
4.6
|
34.4
|
1.0
|
|
C22
|
A:PW2502
|
4.7
|
31.6
|
1.0
|
|
CB
|
A:ASP315
|
4.7
|
48.3
|
1.0
|
|
C03
|
A:PW2502
|
4.7
|
34.5
|
1.0
|
|
HG21
|
C:VAL401
|
4.7
|
66.4
|
1.0
|
|
H221
|
A:PW2502
|
4.8
|
37.9
|
1.0
|
|
HG21
|
A:THR325
|
4.8
|
48.6
|
1.0
|
|
HD1
|
A:HIS313
|
4.8
|
41.7
|
1.0
|
|
HE1
|
A:PHE366
|
4.8
|
42.1
|
1.0
|
|
HD11
|
A:ILE327
|
4.9
|
44.4
|
1.0
|
|
HG22
|
C:VAL401
|
4.9
|
66.4
|
1.0
|
|
CZ
|
A:PHE366
|
4.9
|
33.5
|
1.0
|
|
O01
|
A:PW2502
|
4.9
|
36.0
|
1.0
|
|
Manganese binding site 2 out
of 6 in 6yvt
Go back to
Manganese Binding Sites List in 6yvt
Manganese binding site 2 out
of 6 in the Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Md-253
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Md-253 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn501
b:29.4
occ:1.00
|
N18
|
B:PW2502
|
2.1
|
37.4
|
1.0
|
|
O26
|
B:PW2502
|
2.3
|
38.0
|
1.0
|
|
O
|
B:HOH607
|
2.3
|
36.5
|
1.0
|
|
OD1
|
B:ASP315
|
2.3
|
32.3
|
1.0
|
|
NE2
|
B:HIS313
|
2.3
|
42.9
|
1.0
|
|
NE2
|
B:HIS374
|
2.3
|
32.0
|
1.0
|
|
C19
|
B:PW2502
|
2.9
|
36.3
|
1.0
|
|
C20
|
B:PW2502
|
2.9
|
38.0
|
1.0
|
|
CE1
|
B:HIS313
|
3.0
|
41.1
|
1.0
|
|
HE1
|
B:HIS313
|
3.0
|
49.4
|
1.0
|
|
C17
|
B:PW2502
|
3.1
|
39.3
|
1.0
|
|
H171
|
B:PW2502
|
3.1
|
47.2
|
1.0
|
|
CD2
|
B:HIS374
|
3.2
|
35.4
|
1.0
|
|
CG
|
B:ASP315
|
3.2
|
38.6
|
1.0
|
|
HD2
|
B:HIS374
|
3.3
|
42.5
|
1.0
|
|
CE1
|
B:HIS374
|
3.4
|
34.1
|
1.0
|
|
OD2
|
B:ASP315
|
3.4
|
37.2
|
1.0
|
|
CD2
|
B:HIS313
|
3.5
|
39.8
|
1.0
|
|
HE1
|
B:HIS374
|
3.6
|
41.0
|
1.0
|
|
HD2
|
B:HIS313
|
3.8
|
47.8
|
1.0
|
|
HG11
|
F:VAL401
|
3.9
|
57.9
|
1.0
|
|
HZ
|
B:PHE366
|
4.0
|
36.6
|
1.0
|
|
HZ2
|
B:TRP389
|
4.1
|
48.2
|
1.0
|
|
C02
|
B:PW2502
|
4.2
|
37.9
|
1.0
|
|
N21
|
B:PW2502
|
4.2
|
43.0
|
1.0
|
|
ND1
|
B:HIS313
|
4.2
|
41.7
|
1.0
|
|
C04
|
B:PW2502
|
4.3
|
41.1
|
1.0
|
|
HG21
|
F:VAL401
|
4.4
|
57.9
|
1.0
|
|
O
|
B:HOH604
|
4.4
|
31.7
|
1.0
|
|
CG
|
B:HIS374
|
4.4
|
36.6
|
1.0
|
|
ND1
|
B:HIS374
|
4.5
|
37.3
|
1.0
|
|
CG
|
B:HIS313
|
4.5
|
36.9
|
1.0
|
|
HA
|
B:ASP315
|
4.5
|
44.4
|
1.0
|
|
HG13
|
F:VAL401
|
4.6
|
57.9
|
1.0
|
|
CB
|
B:ASP315
|
4.6
|
40.5
|
1.0
|
|
CG1
|
F:VAL401
|
4.7
|
48.2
|
1.0
|
|
H222
|
B:PW2502
|
4.7
|
49.1
|
1.0
|
|
HG21
|
B:THR325
|
4.8
|
53.8
|
1.0
|
|
H211
|
B:PW2502
|
4.8
|
51.7
|
1.0
|
|
C03
|
B:PW2502
|
4.8
|
38.5
|
1.0
|
|
CZ
|
B:PHE366
|
4.9
|
30.4
|
1.0
|
|
HE1
|
B:PHE366
|
4.9
|
42.2
|
1.0
|
|
C22
|
B:PW2502
|
4.9
|
40.9
|
1.0
|
|
HD1
|
B:HIS313
|
5.0
|
50.1
|
1.0
|
|
CA
|
B:ASP315
|
5.0
|
37.0
|
1.0
|
|
Manganese binding site 3 out
of 6 in 6yvt
Go back to
Manganese Binding Sites List in 6yvt
Manganese binding site 3 out
of 6 in the Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Md-253
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 3 of Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Md-253 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn501
b:32.4
occ:1.00
|
O
|
C:HOH607
|
1.9
|
26.4
|
1.0
|
|
OD1
|
C:ASP315
|
2.2
|
38.0
|
1.0
|
|
NE2
|
C:HIS313
|
2.2
|
35.1
|
1.0
|
|
N18
|
C:PW2502
|
2.2
|
41.1
|
1.0
|
|
O26
|
C:PW2502
|
2.4
|
37.0
|
1.0
|
|
NE2
|
C:HIS374
|
2.4
|
41.7
|
1.0
|
|
CE1
|
C:HIS313
|
3.0
|
34.7
|
1.0
|
|
HE1
|
C:HIS313
|
3.0
|
41.7
|
1.0
|
|
C19
|
C:PW2502
|
3.0
|
36.2
|
1.0
|
|
C20
|
C:PW2502
|
3.0
|
32.5
|
1.0
|
|
CD2
|
C:HIS374
|
3.2
|
32.1
|
1.0
|
|
C17
|
C:PW2502
|
3.2
|
34.8
|
1.0
|
|
HD2
|
C:HIS374
|
3.2
|
38.5
|
1.0
|
|
CG
|
C:ASP315
|
3.2
|
35.6
|
1.0
|
|
H171
|
C:PW2502
|
3.2
|
41.8
|
1.0
|
|
CD2
|
C:HIS313
|
3.4
|
36.7
|
1.0
|
|
CE1
|
C:HIS374
|
3.4
|
36.6
|
1.0
|
|
OD2
|
C:ASP315
|
3.5
|
30.4
|
1.0
|
|
HD2
|
C:HIS313
|
3.7
|
44.1
|
1.0
|
|
HE1
|
C:HIS374
|
3.7
|
44.0
|
1.0
|
|
HZ2
|
C:TRP389
|
4.1
|
44.3
|
1.0
|
|
HG11
|
D:VAL401
|
4.1
|
51.8
|
1.0
|
|
ND1
|
C:HIS313
|
4.2
|
34.6
|
1.0
|
|
HZ
|
C:PHE366
|
4.2
|
49.7
|
1.0
|
|
HA
|
C:ASP315
|
4.3
|
40.7
|
1.0
|
|
C02
|
C:PW2502
|
4.3
|
36.8
|
1.0
|
|
O
|
C:HOH603
|
4.4
|
30.2
|
1.0
|
|
CG
|
C:HIS374
|
4.4
|
31.2
|
1.0
|
|
CG
|
C:HIS313
|
4.4
|
35.6
|
1.0
|
|
N21
|
C:PW2502
|
4.4
|
37.2
|
1.0
|
|
C04
|
C:PW2502
|
4.5
|
34.1
|
1.0
|
|
ND1
|
C:HIS374
|
4.5
|
35.8
|
1.0
|
|
HG22
|
D:VAL401
|
4.5
|
54.3
|
1.0
|
|
HG21
|
C:THR325
|
4.6
|
38.1
|
1.0
|
|
CB
|
C:ASP315
|
4.6
|
40.6
|
1.0
|
|
HE2
|
C:PHE366
|
4.7
|
47.1
|
1.0
|
|
H222
|
C:PW2502
|
4.8
|
37.5
|
1.0
|
|
CA
|
C:ASP315
|
4.8
|
33.8
|
1.0
|
|
H
|
C:ASP315
|
4.9
|
41.4
|
1.0
|
|
HG21
|
D:VAL401
|
4.9
|
54.3
|
1.0
|
|
HD1
|
C:HIS313
|
4.9
|
41.5
|
1.0
|
|
HD11
|
C:ILE327
|
4.9
|
41.5
|
1.0
|
|
C03
|
C:PW2502
|
5.0
|
36.1
|
1.0
|
|
H211
|
C:PW2502
|
5.0
|
44.8
|
1.0
|
|
CZ
|
C:PHE366
|
5.0
|
41.4
|
1.0
|
|
CZ2
|
C:TRP389
|
5.0
|
36.9
|
1.0
|
|
N
|
C:ASP315
|
5.0
|
34.5
|
1.0
|
|
Manganese binding site 4 out
of 6 in 6yvt
Go back to
Manganese Binding Sites List in 6yvt
Manganese binding site 4 out
of 6 in the Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Md-253
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 4 of Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Md-253 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mn501
b:26.8
occ:1.00
|
NE2
|
D:HIS313
|
2.0
|
37.1
|
1.0
|
|
OD1
|
D:ASP315
|
2.2
|
30.4
|
1.0
|
|
O
|
D:HOH606
|
2.3
|
26.9
|
1.0
|
|
N18
|
D:PW2502
|
2.3
|
35.5
|
1.0
|
|
O26
|
D:PW2502
|
2.3
|
31.7
|
1.0
|
|
NE2
|
D:HIS374
|
2.3
|
29.4
|
1.0
|
|
CE1
|
D:HIS313
|
2.7
|
30.9
|
1.0
|
|
HE1
|
D:HIS313
|
2.7
|
37.2
|
1.0
|
|
C20
|
D:PW2502
|
3.0
|
31.7
|
1.0
|
|
C19
|
D:PW2502
|
3.0
|
33.1
|
1.0
|
|
CE1
|
D:HIS374
|
3.2
|
29.7
|
1.0
|
|
CD2
|
D:HIS313
|
3.2
|
32.5
|
1.0
|
|
C17
|
D:PW2502
|
3.2
|
38.8
|
1.0
|
|
CD2
|
D:HIS374
|
3.3
|
32.2
|
1.0
|
|
H171
|
D:PW2502
|
3.3
|
46.6
|
1.0
|
|
CG
|
D:ASP315
|
3.3
|
36.3
|
1.0
|
|
HE1
|
D:HIS374
|
3.3
|
35.7
|
1.0
|
|
HD2
|
D:HIS374
|
3.5
|
38.7
|
1.0
|
|
HD2
|
D:HIS313
|
3.6
|
39.1
|
1.0
|
|
OD2
|
D:ASP315
|
3.7
|
37.1
|
1.0
|
|
HG11
|
A:VAL401
|
3.8
|
43.1
|
1.0
|
|
HZ
|
D:PHE366
|
3.9
|
32.8
|
1.0
|
|
ND1
|
D:HIS313
|
3.9
|
32.1
|
1.0
|
|
CG
|
D:HIS313
|
4.2
|
29.7
|
1.0
|
|
HA
|
D:ASP315
|
4.3
|
41.8
|
1.0
|
|
ND1
|
D:HIS374
|
4.3
|
28.0
|
1.0
|
|
HG13
|
A:VAL401
|
4.4
|
43.1
|
1.0
|
|
HG21
|
A:VAL401
|
4.4
|
41.7
|
1.0
|
|
CG
|
D:HIS374
|
4.4
|
33.1
|
1.0
|
|
C02
|
D:PW2502
|
4.4
|
34.5
|
1.0
|
|
N21
|
D:PW2502
|
4.4
|
31.9
|
1.0
|
|
HZ2
|
D:TRP389
|
4.4
|
34.1
|
1.0
|
|
C04
|
D:PW2502
|
4.5
|
33.6
|
1.0
|
|
CG1
|
A:VAL401
|
4.6
|
35.9
|
1.0
|
|
CB
|
D:ASP315
|
4.6
|
34.0
|
1.0
|
|
HD1
|
D:HIS313
|
4.6
|
38.5
|
1.0
|
|
H222
|
D:PW2502
|
4.7
|
43.5
|
1.0
|
|
CZ
|
D:PHE366
|
4.8
|
27.3
|
1.0
|
|
CA
|
D:ASP315
|
4.8
|
34.8
|
1.0
|
|
H
|
D:ASP315
|
4.9
|
42.8
|
1.0
|
|
N
|
D:ASP315
|
4.9
|
35.6
|
1.0
|
|
HG21
|
D:THR325
|
5.0
|
36.7
|
1.0
|
|
Manganese binding site 5 out
of 6 in 6yvt
Go back to
Manganese Binding Sites List in 6yvt
Manganese binding site 5 out
of 6 in the Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Md-253
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 5 of Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Md-253 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mn501
b:31.4
occ:1.00
|
NE2
|
E:HIS313
|
2.0
|
41.0
|
1.0
|
|
NE2
|
E:HIS374
|
2.3
|
37.3
|
1.0
|
|
O26
|
E:PW2502
|
2.3
|
28.4
|
1.0
|
|
OD1
|
E:ASP315
|
2.4
|
32.0
|
1.0
|
|
O
|
E:HOH609
|
2.4
|
32.4
|
1.0
|
|
N18
|
E:PW2502
|
2.4
|
34.2
|
1.0
|
|
CE1
|
E:HIS313
|
2.7
|
40.7
|
1.0
|
|
HE1
|
E:HIS313
|
2.7
|
48.9
|
1.0
|
|
C20
|
E:PW2502
|
3.0
|
33.5
|
1.0
|
|
CE1
|
E:HIS374
|
3.1
|
33.3
|
1.0
|
|
C19
|
E:PW2502
|
3.2
|
35.4
|
1.0
|
|
CD2
|
E:HIS313
|
3.2
|
40.9
|
1.0
|
|
CD2
|
E:HIS374
|
3.2
|
31.6
|
1.0
|
|
HE1
|
E:HIS374
|
3.2
|
40.0
|
1.0
|
|
C17
|
E:PW2502
|
3.4
|
32.0
|
1.0
|
|
H171
|
E:PW2502
|
3.4
|
38.5
|
1.0
|
|
CG
|
E:ASP315
|
3.4
|
35.9
|
1.0
|
|
HD2
|
E:HIS374
|
3.5
|
38.0
|
1.0
|
|
HD2
|
E:HIS313
|
3.5
|
49.1
|
1.0
|
|
HG11
|
B:VAL401
|
3.7
|
55.7
|
1.0
|
|
ND1
|
E:HIS313
|
3.8
|
41.4
|
1.0
|
|
OD2
|
E:ASP315
|
3.9
|
32.5
|
1.0
|
|
CG
|
E:HIS313
|
4.1
|
40.9
|
1.0
|
|
ND1
|
E:HIS374
|
4.2
|
29.1
|
1.0
|
|
HG21
|
B:VAL401
|
4.2
|
58.8
|
1.0
|
|
HZ
|
E:PHE366
|
4.2
|
46.4
|
1.0
|
|
HA
|
E:ASP315
|
4.3
|
47.4
|
1.0
|
|
CG
|
E:HIS374
|
4.3
|
27.2
|
1.0
|
|
HZ2
|
E:TRP389
|
4.3
|
48.3
|
1.0
|
|
N21
|
E:PW2502
|
4.4
|
28.6
|
1.0
|
|
C02
|
E:PW2502
|
4.5
|
32.9
|
1.0
|
|
HD1
|
E:HIS313
|
4.6
|
49.8
|
1.0
|
|
CG1
|
B:VAL401
|
4.6
|
46.3
|
1.0
|
|
HG13
|
B:VAL401
|
4.6
|
55.7
|
1.0
|
|
O
|
E:HOH607
|
4.7
|
33.1
|
1.0
|
|
CB
|
E:ASP315
|
4.7
|
39.0
|
1.0
|
|
C04
|
E:PW2502
|
4.7
|
31.8
|
1.0
|
|
CA
|
E:ASP315
|
4.8
|
39.5
|
1.0
|
|
H
|
E:ASP315
|
4.8
|
36.4
|
1.0
|
|
HE1
|
E:PHE366
|
4.9
|
39.0
|
1.0
|
|
H222
|
E:PW2502
|
4.9
|
33.0
|
1.0
|
|
N
|
E:ASP315
|
4.9
|
30.3
|
1.0
|
|
HD1
|
E:HIS374
|
4.9
|
34.9
|
1.0
|
|
HG21
|
E:THR325
|
5.0
|
41.6
|
1.0
|
|
Manganese binding site 6 out
of 6 in 6yvt
Go back to
Manganese Binding Sites List in 6yvt
Manganese binding site 6 out
of 6 in the Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Md-253
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 6 of Hif Prolyl Hydroxylase 2 (PHD2/ EGLN1) in Complex with Md-253 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Mn501
b:36.7
occ:1.00
|
N18
|
F:PW2502
|
2.1
|
39.4
|
1.0
|
|
O26
|
F:PW2502
|
2.1
|
39.3
|
1.0
|
|
NE2
|
F:HIS374
|
2.3
|
33.9
|
1.0
|
|
OD1
|
F:ASP315
|
2.3
|
39.8
|
1.0
|
|
NE2
|
F:HIS313
|
2.4
|
35.1
|
1.0
|
|
O
|
F:HOH605
|
2.6
|
30.8
|
1.0
|
|
C20
|
F:PW2502
|
2.8
|
37.9
|
1.0
|
|
C19
|
F:PW2502
|
2.8
|
39.3
|
1.0
|
|
C17
|
F:PW2502
|
3.1
|
37.5
|
1.0
|
|
H171
|
F:PW2502
|
3.2
|
45.0
|
1.0
|
|
CG
|
F:ASP315
|
3.3
|
35.5
|
1.0
|
|
CE1
|
F:HIS313
|
3.3
|
34.8
|
1.0
|
|
CD2
|
F:HIS374
|
3.3
|
31.7
|
1.0
|
|
CE1
|
F:HIS374
|
3.3
|
34.3
|
1.0
|
|
HE1
|
F:HIS313
|
3.3
|
41.8
|
1.0
|
|
HD2
|
F:HIS374
|
3.4
|
38.1
|
1.0
|
|
CD2
|
F:HIS313
|
3.5
|
35.7
|
1.0
|
|
OD2
|
F:ASP315
|
3.5
|
38.5
|
1.0
|
|
HE1
|
F:HIS374
|
3.5
|
41.2
|
1.0
|
|
HD2
|
F:HIS313
|
3.7
|
42.9
|
1.0
|
|
HG11
|
E:VAL401
|
3.9
|
59.0
|
1.0
|
|
HZ
|
F:PHE366
|
3.9
|
44.5
|
1.0
|
|
HZ2
|
F:TRP389
|
4.1
|
48.8
|
1.0
|
|
C02
|
F:PW2502
|
4.1
|
35.8
|
1.0
|
|
N21
|
F:PW2502
|
4.2
|
37.2
|
1.0
|
|
C04
|
F:PW2502
|
4.4
|
37.1
|
1.0
|
|
ND1
|
F:HIS374
|
4.4
|
39.0
|
1.0
|
|
HA
|
F:ASP315
|
4.4
|
50.5
|
1.0
|
|
ND1
|
F:HIS313
|
4.4
|
34.3
|
1.0
|
|
CG
|
F:HIS374
|
4.4
|
37.0
|
1.0
|
|
HG21
|
E:VAL401
|
4.5
|
42.9
|
1.0
|
|
CG
|
F:HIS313
|
4.6
|
35.8
|
1.0
|
|
HG21
|
F:THR325
|
4.6
|
36.0
|
1.0
|
|
H222
|
F:PW2502
|
4.6
|
42.0
|
1.0
|
|
CB
|
F:ASP315
|
4.6
|
36.9
|
1.0
|
|
HG13
|
E:VAL401
|
4.7
|
59.0
|
1.0
|
|
CG1
|
E:VAL401
|
4.7
|
49.1
|
1.0
|
|
H211
|
F:PW2502
|
4.8
|
44.7
|
1.0
|
|
C03
|
F:PW2502
|
4.8
|
40.4
|
1.0
|
|
CZ
|
F:PHE366
|
4.8
|
37.0
|
1.0
|
|
C22
|
F:PW2502
|
4.9
|
35.0
|
1.0
|
|
CA
|
F:ASP315
|
5.0
|
42.0
|
1.0
|
|
CZ2
|
F:TRP389
|
5.0
|
40.6
|
1.0
|
|
H
|
F:ASP315
|
5.0
|
59.8
|
1.0
|
|
Reference:
M.Demetriades,
I.K.Leung,
R.Chowdhury,
M.C.Chan,
M.A.Mcdonough,
K.K.Yeoh,
Y.M.Tian,
T.D.Claridge,
P.J.Ratcliffe,
E.C.Woon,
C.J.Schofield.
Dynamic Combinatorial Chemistry Employing Boronic Acids/Boronate Esters Leads to Potent Oxygenase Inhibitors. Angew.Chem.Int.Ed.Engl. V. 51 6672 2012.
ISSN: ESSN 1521-3773
PubMed: 22639232
DOI: 10.1002/ANIE.201202000
Page generated: Sun Oct 6 07:54:57 2024
|
