Zinc in PDB 5i43: Crystal Structure of the Catalytic Domain of Mmp-12 in Complex with A Selective Sugar-Conjugated Triazole-Linked Carboxylate Chelator Water-Soluble Inhibitor (DC32).
Enzymatic activity of Crystal Structure of the Catalytic Domain of Mmp-12 in Complex with A Selective Sugar-Conjugated Triazole-Linked Carboxylate Chelator Water-Soluble Inhibitor (DC32).
All present enzymatic activity of Crystal Structure of the Catalytic Domain of Mmp-12 in Complex with A Selective Sugar-Conjugated Triazole-Linked Carboxylate Chelator Water-Soluble Inhibitor (DC32).:
3.4.24.65;
Protein crystallography data
The structure of Crystal Structure of the Catalytic Domain of Mmp-12 in Complex with A Selective Sugar-Conjugated Triazole-Linked Carboxylate Chelator Water-Soluble Inhibitor (DC32)., PDB code: 5i43
was solved by
E.A.Stura,
L.Rosalia,
D.Cuffaro,
L.Tepshi,
L.Ciccone,
A.Rossello,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
44.56 /
1.95
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
64.030,
63.660,
79.030,
90.00,
103.03,
90.00
|
R / Rfree (%)
|
20 /
23.3
|
Other elements in 5i43:
The structure of Crystal Structure of the Catalytic Domain of Mmp-12 in Complex with A Selective Sugar-Conjugated Triazole-Linked Carboxylate Chelator Water-Soluble Inhibitor (DC32). also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of the Catalytic Domain of Mmp-12 in Complex with A Selective Sugar-Conjugated Triazole-Linked Carboxylate Chelator Water-Soluble Inhibitor (DC32).
(pdb code 5i43). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 8 binding sites of Zinc where determined in the
Crystal Structure of the Catalytic Domain of Mmp-12 in Complex with A Selective Sugar-Conjugated Triazole-Linked Carboxylate Chelator Water-Soluble Inhibitor (DC32)., PDB code: 5i43:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Zinc binding site 1 out
of 8 in 5i43
Go back to
Zinc Binding Sites List in 5i43
Zinc binding site 1 out
of 8 in the Crystal Structure of the Catalytic Domain of Mmp-12 in Complex with A Selective Sugar-Conjugated Triazole-Linked Carboxylate Chelator Water-Soluble Inhibitor (DC32).
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Crystal Structure of the Catalytic Domain of Mmp-12 in Complex with A Selective Sugar-Conjugated Triazole-Linked Carboxylate Chelator Water-Soluble Inhibitor (DC32). within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn301
b:17.6
occ:1.00
|
O20
|
A:67M306
|
1.9
|
21.1
|
1.0
|
NE2
|
A:HIS218
|
2.1
|
23.0
|
1.0
|
NE2
|
A:HIS228
|
2.1
|
21.8
|
1.0
|
NE2
|
A:HIS222
|
2.1
|
15.3
|
1.0
|
O19
|
A:67M306
|
2.6
|
24.8
|
1.0
|
C18
|
A:67M306
|
2.6
|
23.6
|
1.0
|
CE1
|
A:HIS218
|
3.0
|
20.1
|
1.0
|
CD2
|
A:HIS218
|
3.0
|
21.6
|
1.0
|
CE1
|
A:HIS222
|
3.1
|
18.4
|
1.0
|
CD2
|
A:HIS228
|
3.1
|
19.2
|
1.0
|
CE1
|
A:HIS228
|
3.1
|
21.5
|
1.0
|
CD2
|
A:HIS222
|
3.1
|
14.3
|
1.0
|
ND1
|
A:HIS218
|
4.1
|
20.1
|
1.0
|
C17
|
A:67M306
|
4.1
|
27.6
|
1.0
|
CG
|
A:HIS218
|
4.1
|
19.7
|
1.0
|
O
|
A:HOH436
|
4.1
|
26.0
|
1.0
|
ND1
|
A:HIS222
|
4.2
|
17.5
|
1.0
|
ND1
|
A:HIS228
|
4.2
|
22.7
|
1.0
|
CG
|
A:HIS228
|
4.2
|
19.4
|
1.0
|
CG
|
A:HIS222
|
4.2
|
18.0
|
1.0
|
N16
|
A:67M306
|
4.7
|
31.4
|
1.0
|
NE2
|
A:GLN219
|
4.7
|
20.8
|
1.0
|
C24
|
A:67M306
|
4.8
|
36.8
|
1.0
|
C23
|
A:67M306
|
4.8
|
34.3
|
1.0
|
C21
|
A:67M306
|
4.8
|
32.0
|
1.0
|
CE
|
A:MET236
|
4.9
|
18.0
|
1.0
|
|
Zinc binding site 2 out
of 8 in 5i43
Go back to
Zinc Binding Sites List in 5i43
Zinc binding site 2 out
of 8 in the Crystal Structure of the Catalytic Domain of Mmp-12 in Complex with A Selective Sugar-Conjugated Triazole-Linked Carboxylate Chelator Water-Soluble Inhibitor (DC32).
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Crystal Structure of the Catalytic Domain of Mmp-12 in Complex with A Selective Sugar-Conjugated Triazole-Linked Carboxylate Chelator Water-Soluble Inhibitor (DC32). within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn302
b:17.5
occ:1.00
|
OD2
|
A:ASP170
|
1.9
|
24.0
|
1.0
|
ND1
|
A:HIS196
|
2.0
|
17.6
|
1.0
|
NE2
|
A:HIS183
|
2.1
|
19.8
|
1.0
|
NE2
|
A:HIS168
|
2.2
|
15.9
|
1.0
|
CG
|
A:ASP170
|
2.8
|
22.8
|
1.0
|
CE1
|
A:HIS196
|
2.9
|
18.1
|
1.0
|
CD2
|
A:HIS168
|
2.9
|
20.2
|
1.0
|
CE1
|
A:HIS183
|
3.0
|
18.1
|
1.0
|
CG
|
A:HIS196
|
3.0
|
16.4
|
1.0
|
CD2
|
A:HIS183
|
3.1
|
20.8
|
1.0
|
OD1
|
A:ASP170
|
3.1
|
17.4
|
1.0
|
CE1
|
A:HIS168
|
3.3
|
19.4
|
1.0
|
CB
|
A:HIS196
|
3.4
|
14.7
|
1.0
|
O
|
A:HOH445
|
3.9
|
7.2
|
0.6
|
NE2
|
A:HIS196
|
4.0
|
15.7
|
1.0
|
ND1
|
A:HIS183
|
4.1
|
18.2
|
1.0
|
CD2
|
A:HIS196
|
4.1
|
15.7
|
1.0
|
CB
|
A:ASP170
|
4.1
|
21.3
|
1.0
|
CG
|
A:HIS168
|
4.2
|
19.1
|
1.0
|
CG
|
A:HIS183
|
4.2
|
15.5
|
1.0
|
ND1
|
A:HIS168
|
4.3
|
18.5
|
1.0
|
CE1
|
A:PHE185
|
4.3
|
27.4
|
1.0
|
O
|
A:HIS172
|
4.3
|
20.4
|
1.0
|
CZ
|
A:PHE174
|
4.5
|
17.3
|
1.0
|
CZ
|
A:PHE185
|
4.6
|
27.0
|
1.0
|
O
|
A:HOH429
|
4.7
|
17.8
|
1.0
|
CE2
|
A:PHE174
|
4.8
|
16.0
|
1.0
|
CA
|
A:HIS196
|
5.0
|
15.3
|
1.0
|
|
Zinc binding site 3 out
of 8 in 5i43
Go back to
Zinc Binding Sites List in 5i43
Zinc binding site 3 out
of 8 in the Crystal Structure of the Catalytic Domain of Mmp-12 in Complex with A Selective Sugar-Conjugated Triazole-Linked Carboxylate Chelator Water-Soluble Inhibitor (DC32).
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Crystal Structure of the Catalytic Domain of Mmp-12 in Complex with A Selective Sugar-Conjugated Triazole-Linked Carboxylate Chelator Water-Soluble Inhibitor (DC32). within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn302
b:20.1
occ:1.00
|
O20
|
B:67M301
|
1.9
|
19.1
|
1.0
|
NE2
|
B:HIS218
|
2.0
|
19.6
|
1.0
|
NE2
|
B:HIS222
|
2.1
|
16.1
|
1.0
|
NE2
|
B:HIS228
|
2.2
|
24.7
|
1.0
|
O19
|
B:67M301
|
2.6
|
29.2
|
1.0
|
C18
|
B:67M301
|
2.6
|
24.8
|
1.0
|
CE1
|
B:HIS218
|
3.0
|
19.3
|
1.0
|
CD2
|
B:HIS222
|
3.0
|
16.9
|
1.0
|
CE1
|
B:HIS222
|
3.1
|
17.9
|
1.0
|
CD2
|
B:HIS218
|
3.1
|
19.6
|
1.0
|
CD2
|
B:HIS228
|
3.2
|
23.2
|
1.0
|
CE1
|
B:HIS228
|
3.2
|
25.1
|
1.0
|
ND1
|
B:HIS218
|
4.1
|
18.8
|
1.0
|
C17
|
B:67M301
|
4.1
|
27.6
|
1.0
|
ND1
|
B:HIS222
|
4.2
|
17.5
|
1.0
|
CG
|
B:HIS218
|
4.2
|
16.8
|
1.0
|
CG
|
B:HIS222
|
4.2
|
18.4
|
1.0
|
ND1
|
B:HIS228
|
4.3
|
20.7
|
1.0
|
CG
|
B:HIS228
|
4.3
|
21.9
|
1.0
|
N16
|
B:67M301
|
4.6
|
29.9
|
1.0
|
C24
|
B:67M301
|
4.7
|
38.3
|
1.0
|
NE2
|
B:GLN219
|
4.7
|
19.8
|
1.0
|
C22
|
B:67M301
|
4.8
|
36.0
|
1.0
|
C09
|
B:67M301
|
4.9
|
27.7
|
1.0
|
C10
|
B:67M301
|
4.9
|
28.3
|
1.0
|
C21
|
B:67M301
|
4.9
|
31.6
|
1.0
|
C08
|
B:67M301
|
5.0
|
27.4
|
1.0
|
|
Zinc binding site 4 out
of 8 in 5i43
Go back to
Zinc Binding Sites List in 5i43
Zinc binding site 4 out
of 8 in the Crystal Structure of the Catalytic Domain of Mmp-12 in Complex with A Selective Sugar-Conjugated Triazole-Linked Carboxylate Chelator Water-Soluble Inhibitor (DC32).
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Crystal Structure of the Catalytic Domain of Mmp-12 in Complex with A Selective Sugar-Conjugated Triazole-Linked Carboxylate Chelator Water-Soluble Inhibitor (DC32). within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn303
b:18.5
occ:1.00
|
OD2
|
B:ASP170
|
1.9
|
17.5
|
1.0
|
NE2
|
B:HIS168
|
2.1
|
17.3
|
1.0
|
NE2
|
B:HIS183
|
2.1
|
18.1
|
1.0
|
ND1
|
B:HIS196
|
2.1
|
21.0
|
1.0
|
CG
|
B:ASP170
|
2.8
|
19.1
|
1.0
|
CD2
|
B:HIS168
|
2.9
|
18.4
|
1.0
|
CE1
|
B:HIS196
|
3.0
|
22.1
|
1.0
|
CE1
|
B:HIS183
|
3.0
|
16.8
|
1.0
|
CE1
|
B:HIS168
|
3.1
|
20.7
|
1.0
|
CD2
|
B:HIS183
|
3.1
|
17.6
|
1.0
|
CG
|
B:HIS196
|
3.2
|
22.0
|
1.0
|
OD1
|
B:ASP170
|
3.2
|
17.8
|
1.0
|
CB
|
B:HIS196
|
3.6
|
17.6
|
1.0
|
CG
|
B:HIS168
|
4.1
|
20.4
|
1.0
|
NE2
|
B:HIS196
|
4.1
|
21.7
|
1.0
|
CB
|
B:ASP170
|
4.1
|
20.3
|
1.0
|
ND1
|
B:HIS183
|
4.1
|
14.2
|
1.0
|
ND1
|
B:HIS168
|
4.2
|
20.6
|
1.0
|
O
|
B:HIS172
|
4.2
|
22.1
|
1.0
|
CG
|
B:HIS183
|
4.2
|
14.9
|
1.0
|
CD2
|
B:HIS196
|
4.3
|
20.9
|
1.0
|
CE1
|
B:PHE185
|
4.4
|
25.7
|
1.0
|
CZ
|
B:PHE174
|
4.6
|
20.8
|
1.0
|
CZ
|
B:PHE185
|
4.7
|
28.1
|
1.0
|
CE2
|
B:PHE174
|
4.8
|
19.4
|
1.0
|
O
|
B:HOH460
|
4.8
|
41.4
|
1.0
|
CB
|
B:HIS172
|
4.9
|
21.6
|
1.0
|
O
|
B:HOH443
|
4.9
|
14.3
|
1.0
|
|
Zinc binding site 5 out
of 8 in 5i43
Go back to
Zinc Binding Sites List in 5i43
Zinc binding site 5 out
of 8 in the Crystal Structure of the Catalytic Domain of Mmp-12 in Complex with A Selective Sugar-Conjugated Triazole-Linked Carboxylate Chelator Water-Soluble Inhibitor (DC32).
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of Crystal Structure of the Catalytic Domain of Mmp-12 in Complex with A Selective Sugar-Conjugated Triazole-Linked Carboxylate Chelator Water-Soluble Inhibitor (DC32). within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn302
b:16.1
occ:1.00
|
O20
|
C:67M301
|
1.9
|
19.4
|
1.0
|
NE2
|
C:HIS222
|
2.1
|
12.5
|
1.0
|
NE2
|
C:HIS228
|
2.1
|
20.5
|
1.0
|
NE2
|
C:HIS218
|
2.1
|
23.3
|
1.0
|
O19
|
C:67M301
|
2.5
|
24.9
|
1.0
|
C18
|
C:67M301
|
2.5
|
21.3
|
1.0
|
CE1
|
C:HIS222
|
3.0
|
15.3
|
1.0
|
CD2
|
C:HIS218
|
3.0
|
20.2
|
1.0
|
CD2
|
C:HIS222
|
3.0
|
13.4
|
1.0
|
CD2
|
C:HIS228
|
3.1
|
19.9
|
1.0
|
CE1
|
C:HIS228
|
3.1
|
19.5
|
1.0
|
CE1
|
C:HIS218
|
3.1
|
20.1
|
1.0
|
C17
|
C:67M301
|
4.0
|
22.3
|
1.0
|
ND1
|
C:HIS222
|
4.1
|
16.5
|
1.0
|
CG
|
C:HIS218
|
4.2
|
18.7
|
1.0
|
CG
|
C:HIS222
|
4.2
|
17.0
|
1.0
|
ND1
|
C:HIS218
|
4.2
|
21.9
|
1.0
|
ND1
|
C:HIS228
|
4.2
|
16.9
|
1.0
|
CG
|
C:HIS228
|
4.2
|
18.4
|
1.0
|
N16
|
C:67M301
|
4.6
|
24.0
|
1.0
|
C24
|
C:67M301
|
4.6
|
30.4
|
1.0
|
C23
|
C:67M301
|
4.7
|
22.7
|
1.0
|
NE2
|
C:GLN219
|
4.7
|
16.4
|
1.0
|
C09
|
C:67M301
|
4.8
|
21.0
|
1.0
|
CE
|
C:MET236
|
4.8
|
19.4
|
1.0
|
O
|
C:HOH519
|
4.8
|
15.2
|
0.4
|
C10
|
C:67M301
|
4.8
|
22.5
|
1.0
|
C21
|
C:67M301
|
4.9
|
22.7
|
1.0
|
O
|
C:HOH519
|
4.9
|
41.0
|
0.6
|
C08
|
C:67M301
|
4.9
|
20.5
|
1.0
|
|
Zinc binding site 6 out
of 8 in 5i43
Go back to
Zinc Binding Sites List in 5i43
Zinc binding site 6 out
of 8 in the Crystal Structure of the Catalytic Domain of Mmp-12 in Complex with A Selective Sugar-Conjugated Triazole-Linked Carboxylate Chelator Water-Soluble Inhibitor (DC32).
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 6 of Crystal Structure of the Catalytic Domain of Mmp-12 in Complex with A Selective Sugar-Conjugated Triazole-Linked Carboxylate Chelator Water-Soluble Inhibitor (DC32). within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn303
b:16.3
occ:1.00
|
OD2
|
C:ASP170
|
1.9
|
18.6
|
1.0
|
ND1
|
C:HIS196
|
2.1
|
15.4
|
1.0
|
NE2
|
C:HIS168
|
2.1
|
12.6
|
1.0
|
NE2
|
C:HIS183
|
2.1
|
15.6
|
1.0
|
CG
|
C:ASP170
|
2.9
|
15.2
|
1.0
|
CE1
|
C:HIS196
|
3.0
|
16.7
|
1.0
|
CE1
|
C:HIS183
|
3.0
|
13.8
|
1.0
|
CD2
|
C:HIS168
|
3.0
|
12.3
|
1.0
|
CE1
|
C:HIS168
|
3.1
|
15.1
|
1.0
|
CG
|
C:HIS196
|
3.2
|
14.9
|
1.0
|
CD2
|
C:HIS183
|
3.2
|
13.2
|
1.0
|
OD1
|
C:ASP170
|
3.3
|
16.8
|
1.0
|
CB
|
C:HIS196
|
3.6
|
14.0
|
1.0
|
NE2
|
C:HIS196
|
4.1
|
15.8
|
1.0
|
CB
|
C:ASP170
|
4.1
|
15.8
|
1.0
|
ND1
|
C:HIS183
|
4.2
|
10.6
|
1.0
|
ND1
|
C:HIS168
|
4.2
|
15.9
|
1.0
|
CG
|
C:HIS168
|
4.2
|
14.3
|
1.0
|
CD2
|
C:HIS196
|
4.2
|
15.3
|
1.0
|
CG
|
C:HIS183
|
4.3
|
11.0
|
1.0
|
O
|
C:HIS172
|
4.3
|
12.7
|
1.0
|
CE1
|
C:PHE185
|
4.4
|
25.1
|
1.0
|
CZ
|
C:PHE185
|
4.5
|
26.0
|
1.0
|
O
|
C:HOH452
|
4.6
|
33.9
|
1.0
|
CZ
|
C:PHE174
|
4.7
|
17.6
|
1.0
|
O
|
C:HOH419
|
4.8
|
9.1
|
1.0
|
CE2
|
C:PHE174
|
4.8
|
15.2
|
1.0
|
CB
|
C:HIS172
|
5.0
|
22.3
|
1.0
|
|
Zinc binding site 7 out
of 8 in 5i43
Go back to
Zinc Binding Sites List in 5i43
Zinc binding site 7 out
of 8 in the Crystal Structure of the Catalytic Domain of Mmp-12 in Complex with A Selective Sugar-Conjugated Triazole-Linked Carboxylate Chelator Water-Soluble Inhibitor (DC32).
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 7 of Crystal Structure of the Catalytic Domain of Mmp-12 in Complex with A Selective Sugar-Conjugated Triazole-Linked Carboxylate Chelator Water-Soluble Inhibitor (DC32). within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn302
b:16.4
occ:1.00
|
O20
|
D:67M301
|
1.8
|
27.2
|
1.0
|
NE2
|
D:HIS222
|
2.0
|
14.0
|
1.0
|
NE2
|
D:HIS218
|
2.1
|
14.3
|
1.0
|
NE2
|
D:HIS228
|
2.1
|
19.4
|
1.0
|
O19
|
D:67M301
|
2.6
|
22.1
|
1.0
|
C18
|
D:67M301
|
2.6
|
24.3
|
1.0
|
CD2
|
D:HIS218
|
2.9
|
13.8
|
1.0
|
CD2
|
D:HIS222
|
3.0
|
13.8
|
1.0
|
CD2
|
D:HIS228
|
3.0
|
18.2
|
1.0
|
CE1
|
D:HIS222
|
3.0
|
17.1
|
1.0
|
CE1
|
D:HIS218
|
3.1
|
14.9
|
1.0
|
CE1
|
D:HIS228
|
3.1
|
19.4
|
1.0
|
O
|
D:HOH428
|
3.8
|
14.1
|
0.6
|
CG
|
D:HIS218
|
4.1
|
12.9
|
1.0
|
C17
|
D:67M301
|
4.1
|
25.3
|
1.0
|
ND1
|
D:HIS222
|
4.1
|
15.1
|
1.0
|
CG
|
D:HIS222
|
4.1
|
15.7
|
1.0
|
ND1
|
D:HIS218
|
4.1
|
15.7
|
1.0
|
CG
|
D:HIS228
|
4.2
|
19.1
|
1.0
|
ND1
|
D:HIS228
|
4.2
|
18.2
|
1.0
|
N16
|
D:67M301
|
4.7
|
27.5
|
1.0
|
C24
|
D:67M301
|
4.7
|
29.9
|
1.0
|
NE2
|
D:GLN219
|
4.8
|
21.3
|
1.0
|
C22
|
D:67M301
|
4.8
|
30.7
|
1.0
|
C21
|
D:67M301
|
4.9
|
28.4
|
1.0
|
CE
|
D:MET236
|
4.9
|
19.5
|
1.0
|
|
Zinc binding site 8 out
of 8 in 5i43
Go back to
Zinc Binding Sites List in 5i43
Zinc binding site 8 out
of 8 in the Crystal Structure of the Catalytic Domain of Mmp-12 in Complex with A Selective Sugar-Conjugated Triazole-Linked Carboxylate Chelator Water-Soluble Inhibitor (DC32).
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 8 of Crystal Structure of the Catalytic Domain of Mmp-12 in Complex with A Selective Sugar-Conjugated Triazole-Linked Carboxylate Chelator Water-Soluble Inhibitor (DC32). within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn303
b:17.3
occ:1.00
|
OD2
|
D:ASP170
|
1.8
|
21.9
|
1.0
|
NE2
|
D:HIS168
|
2.0
|
15.1
|
1.0
|
NE2
|
D:HIS183
|
2.1
|
16.5
|
1.0
|
ND1
|
D:HIS196
|
2.1
|
16.1
|
1.0
|
CG
|
D:ASP170
|
2.8
|
20.9
|
1.0
|
CD2
|
D:HIS168
|
2.8
|
14.7
|
1.0
|
CE1
|
D:HIS183
|
2.9
|
16.2
|
1.0
|
CE1
|
D:HIS196
|
3.0
|
16.4
|
1.0
|
CG
|
D:HIS196
|
3.1
|
16.1
|
1.0
|
CD2
|
D:HIS183
|
3.1
|
17.0
|
1.0
|
CE1
|
D:HIS168
|
3.2
|
17.4
|
1.0
|
OD1
|
D:ASP170
|
3.2
|
17.9
|
1.0
|
CB
|
D:HIS196
|
3.5
|
14.5
|
1.0
|
CG
|
D:HIS168
|
4.1
|
15.9
|
1.0
|
ND1
|
D:HIS183
|
4.1
|
15.8
|
1.0
|
CB
|
D:ASP170
|
4.1
|
19.9
|
1.0
|
NE2
|
D:HIS196
|
4.1
|
15.9
|
1.0
|
O
|
D:HIS172
|
4.2
|
14.3
|
1.0
|
ND1
|
D:HIS168
|
4.2
|
16.4
|
1.0
|
CD2
|
D:HIS196
|
4.2
|
16.9
|
1.0
|
CG
|
D:HIS183
|
4.2
|
14.8
|
1.0
|
CE1
|
D:PHE185
|
4.4
|
23.0
|
1.0
|
O
|
D:HOH411
|
4.6
|
12.6
|
1.0
|
CZ
|
D:PHE174
|
4.6
|
17.8
|
1.0
|
CZ
|
D:PHE185
|
4.8
|
21.6
|
1.0
|
CE2
|
D:PHE174
|
4.8
|
19.7
|
1.0
|
|
Reference:
E.Nuti,
D.Cuffaro,
F.D'andrea,
L.Rosalia,
L.Tepshi,
M.Fabbi,
G.Carbotti,
S.Ferrini,
S.Santamaria,
C.Camodeca,
L.Ciccone,
E.Orlandini,
S.Nencetti,
E.A.Stura,
V.Dive,
A.Rossello.
Sugar-Based Arylsulfonamide Carboxylates As Selective and Water-Soluble Matrix Metalloproteinase-12 Inhibitors. Chemmedchem V. 11 1626 2016.
ISSN: ESSN 1860-7187
PubMed: 27356908
DOI: 10.1002/CMDC.201600235
Page generated: Sun Oct 27 17:54:06 2024
|