Zinc in PDB 4h82: Crystal Structure of Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor.
Enzymatic activity of Crystal Structure of Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor.
All present enzymatic activity of Crystal Structure of Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor.:
3.4.24.35;
Protein crystallography data
The structure of Crystal Structure of Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor., PDB code: 4h82
was solved by
C.Antoni,
E.A.Stura,
L.Vera,
E.Cassar-Lajeunesse,
E.Nuti,
V.Dive,
A.Rossello,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
33.46 /
1.90
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
39.900,
98.860,
47.130,
90.03,
111.95,
89.98
|
R / Rfree (%)
|
20.7 /
24.1
|
Other elements in 4h82:
The structure of Crystal Structure of Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor. also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor.
(pdb code 4h82). 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 Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor., PDB code: 4h82:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Zinc binding site 1 out
of 8 in 4h82
Go back to
Zinc Binding Sites List in 4h82
Zinc binding site 1 out
of 8 in the Crystal Structure of Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor.
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 Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn301
b:12.1
occ:1.00
|
O23
|
A:L29306
|
1.9
|
11.1
|
1.0
|
O22
|
A:L29306
|
1.9
|
13.3
|
1.0
|
NE2
|
A:HIS226
|
2.0
|
16.4
|
1.0
|
NE2
|
A:HIS236
|
2.2
|
14.4
|
1.0
|
NE2
|
A:HIS230
|
2.4
|
8.0
|
1.0
|
C21
|
A:L29306
|
2.5
|
21.7
|
1.0
|
N22
|
A:L29306
|
2.6
|
17.1
|
1.0
|
CD2
|
A:HIS226
|
2.8
|
16.5
|
1.0
|
CE1
|
A:HIS226
|
3.1
|
8.8
|
1.0
|
CE1
|
A:HIS236
|
3.1
|
12.4
|
1.0
|
CD2
|
A:HIS236
|
3.2
|
12.6
|
1.0
|
CD2
|
A:HIS230
|
3.3
|
5.3
|
1.0
|
CE1
|
A:HIS230
|
3.4
|
14.3
|
1.0
|
C17
|
A:L29306
|
4.0
|
9.7
|
1.0
|
O
|
A:HOH427
|
4.0
|
8.1
|
1.0
|
CG
|
A:HIS226
|
4.0
|
10.6
|
1.0
|
ND1
|
A:HIS226
|
4.1
|
12.4
|
1.0
|
ND1
|
A:HIS236
|
4.2
|
11.7
|
1.0
|
C11
|
A:L29306
|
4.2
|
7.4
|
1.0
|
CG
|
A:HIS236
|
4.3
|
9.7
|
1.0
|
C12
|
A:L29306
|
4.3
|
7.0
|
1.0
|
CG
|
A:HIS230
|
4.5
|
7.5
|
1.0
|
ND1
|
A:HIS230
|
4.5
|
3.2
|
1.0
|
C10
|
A:L29306
|
4.7
|
7.5
|
1.0
|
C24
|
A:L29306
|
4.7
|
15.4
|
1.0
|
N16
|
A:L29306
|
4.7
|
14.4
|
1.0
|
C18
|
A:L29306
|
4.8
|
12.1
|
1.0
|
NE2
|
A:GLN227
|
4.8
|
7.8
|
1.0
|
C7
|
A:L29306
|
4.8
|
6.6
|
1.0
|
C20
|
A:L29306
|
5.0
|
8.8
|
1.0
|
CE
|
A:MET244
|
5.0
|
9.4
|
1.0
|
C19
|
A:L29306
|
5.0
|
17.8
|
1.0
|
|
Zinc binding site 2 out
of 8 in 4h82
Go back to
Zinc Binding Sites List in 4h82
Zinc binding site 2 out
of 8 in the Crystal Structure of Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor.
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 Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn302
b:17.2
occ:1.00
|
OD2
|
A:ASP177
|
1.9
|
12.9
|
1.0
|
NE2
|
A:HIS175
|
2.0
|
4.2
|
1.0
|
ND1
|
A:HIS203
|
2.1
|
10.2
|
1.0
|
NE2
|
A:HIS190
|
2.1
|
16.9
|
1.0
|
CG
|
A:ASP177
|
2.7
|
19.1
|
1.0
|
CE1
|
A:HIS203
|
2.8
|
7.5
|
1.0
|
CD2
|
A:HIS175
|
2.8
|
17.8
|
1.0
|
OD1
|
A:ASP177
|
2.9
|
13.3
|
1.0
|
CE1
|
A:HIS190
|
2.9
|
16.0
|
1.0
|
CE1
|
A:HIS175
|
3.1
|
22.5
|
1.0
|
CD2
|
A:HIS190
|
3.3
|
13.0
|
1.0
|
CG
|
A:HIS203
|
3.3
|
11.8
|
1.0
|
CB
|
A:HIS203
|
3.9
|
6.3
|
1.0
|
NE2
|
A:HIS203
|
4.0
|
6.0
|
1.0
|
CG
|
A:HIS175
|
4.1
|
14.3
|
1.0
|
CB
|
A:ASP177
|
4.1
|
12.2
|
1.0
|
ND1
|
A:HIS190
|
4.1
|
5.2
|
1.0
|
ND1
|
A:HIS175
|
4.1
|
12.5
|
1.0
|
CE1
|
A:PHE192
|
4.2
|
12.9
|
1.0
|
O
|
A:TYR179
|
4.3
|
21.6
|
1.0
|
CD2
|
A:HIS203
|
4.3
|
7.7
|
1.0
|
CG
|
A:HIS190
|
4.3
|
14.3
|
1.0
|
CZ
|
A:PHE181
|
4.4
|
14.6
|
1.0
|
CE1
|
A:PHE181
|
4.6
|
15.9
|
1.0
|
CZ
|
A:PHE192
|
4.7
|
13.7
|
1.0
|
CB
|
A:TYR179
|
4.8
|
11.1
|
1.0
|
N
|
A:ASP177
|
4.9
|
18.4
|
1.0
|
|
Zinc binding site 3 out
of 8 in 4h82
Go back to
Zinc Binding Sites List in 4h82
Zinc binding site 3 out
of 8 in the Crystal Structure of Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor.
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 Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn300
b:10.1
occ:1.00
|
NE2
|
B:HIS226
|
2.0
|
3.8
|
1.0
|
NE2
|
B:HIS236
|
2.0
|
9.8
|
1.0
|
O61
|
A:L29306
|
2.1
|
24.7
|
1.0
|
O62
|
A:L29306
|
2.1
|
20.9
|
1.0
|
NE2
|
B:HIS230
|
2.5
|
6.5
|
1.0
|
CD2
|
B:HIS236
|
2.7
|
16.0
|
1.0
|
C60
|
A:L29306
|
2.8
|
12.2
|
1.0
|
CD2
|
B:HIS230
|
2.8
|
7.3
|
1.0
|
N61
|
A:L29306
|
2.8
|
10.3
|
1.0
|
CE1
|
B:HIS226
|
2.8
|
7.6
|
1.0
|
CD2
|
B:HIS226
|
3.1
|
7.5
|
1.0
|
CE1
|
B:HIS236
|
3.2
|
10.2
|
1.0
|
CE1
|
B:HIS230
|
3.8
|
10.7
|
1.0
|
CG
|
B:HIS236
|
4.0
|
9.4
|
1.0
|
ND1
|
B:HIS226
|
4.0
|
11.0
|
1.0
|
CG
|
B:HIS230
|
4.1
|
14.1
|
1.0
|
ND1
|
B:HIS236
|
4.2
|
8.5
|
1.0
|
CG
|
B:HIS226
|
4.2
|
6.6
|
1.0
|
C56
|
A:L29306
|
4.2
|
14.6
|
1.0
|
O
|
B:HOH401
|
4.2
|
6.2
|
1.0
|
NE2
|
B:GLN227
|
4.6
|
2.2
|
1.0
|
C5A
|
A:L29306
|
4.6
|
8.1
|
1.0
|
ND1
|
B:HIS230
|
4.6
|
7.2
|
1.0
|
C49
|
A:L29306
|
4.6
|
7.9
|
1.0
|
C57
|
A:L29306
|
4.8
|
10.5
|
1.0
|
C39
|
A:L29306
|
4.8
|
16.3
|
1.0
|
CE
|
B:MET244
|
4.8
|
6.4
|
1.0
|
C58
|
A:L29306
|
4.9
|
7.2
|
1.0
|
C45
|
A:L29306
|
5.0
|
10.1
|
1.0
|
|
Zinc binding site 4 out
of 8 in 4h82
Go back to
Zinc Binding Sites List in 4h82
Zinc binding site 4 out
of 8 in the Crystal Structure of Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor.
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 Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn301
b:22.1
occ:1.00
|
OD2
|
B:ASP177
|
1.9
|
10.3
|
1.0
|
NE2
|
B:HIS175
|
2.1
|
14.2
|
1.0
|
ND1
|
B:HIS203
|
2.2
|
13.6
|
1.0
|
CG
|
B:ASP177
|
2.4
|
18.2
|
1.0
|
OD1
|
B:ASP177
|
2.6
|
24.1
|
1.0
|
NE2
|
B:HIS190
|
2.6
|
15.6
|
1.0
|
CD2
|
B:HIS175
|
2.9
|
16.8
|
1.0
|
CE1
|
B:HIS175
|
3.0
|
16.1
|
1.0
|
CG
|
B:HIS203
|
3.1
|
14.3
|
1.0
|
CB
|
B:HIS203
|
3.2
|
14.6
|
1.0
|
CE1
|
B:HIS190
|
3.2
|
14.0
|
1.0
|
CE1
|
B:HIS203
|
3.3
|
9.9
|
1.0
|
CB
|
B:ASP177
|
3.6
|
21.8
|
1.0
|
CD2
|
B:HIS190
|
3.7
|
6.1
|
1.0
|
CG
|
B:HIS175
|
4.0
|
15.3
|
1.0
|
ND1
|
B:HIS175
|
4.0
|
16.7
|
1.0
|
CE2
|
B:PHE181
|
4.2
|
15.7
|
1.0
|
CD2
|
B:HIS203
|
4.3
|
6.8
|
1.0
|
CZ
|
B:PHE192
|
4.3
|
13.8
|
1.0
|
NE2
|
B:HIS203
|
4.4
|
10.8
|
1.0
|
ND1
|
B:HIS190
|
4.4
|
15.6
|
1.0
|
O
|
B:TYR179
|
4.5
|
21.4
|
1.0
|
CZ
|
B:PHE181
|
4.5
|
11.1
|
1.0
|
CG
|
B:HIS190
|
4.7
|
11.3
|
1.0
|
CA
|
B:HIS203
|
4.7
|
13.6
|
1.0
|
CE1
|
B:PHE192
|
4.8
|
9.4
|
1.0
|
CA
|
B:ASP177
|
4.8
|
19.2
|
1.0
|
N
|
B:ASP177
|
4.8
|
13.0
|
1.0
|
|
Zinc binding site 5 out
of 8 in 4h82
Go back to
Zinc Binding Sites List in 4h82
Zinc binding site 5 out
of 8 in the Crystal Structure of Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor.
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 Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn301
b:11.2
occ:1.00
|
NE2
|
C:HIS226
|
2.0
|
9.0
|
1.0
|
O23
|
D:L29303
|
2.1
|
15.0
|
1.0
|
NE2
|
C:HIS236
|
2.1
|
11.3
|
1.0
|
NE2
|
C:HIS230
|
2.2
|
4.5
|
1.0
|
O22
|
D:L29303
|
2.2
|
26.1
|
1.0
|
CD2
|
C:HIS230
|
2.7
|
8.1
|
1.0
|
CD2
|
C:HIS226
|
2.7
|
16.0
|
1.0
|
C21
|
D:L29303
|
2.8
|
16.6
|
1.0
|
N22
|
D:L29303
|
2.9
|
15.2
|
1.0
|
CD2
|
C:HIS236
|
2.9
|
9.4
|
1.0
|
CE1
|
C:HIS226
|
3.2
|
7.4
|
1.0
|
CE1
|
C:HIS236
|
3.2
|
11.4
|
1.0
|
CE1
|
C:HIS230
|
3.4
|
14.6
|
1.0
|
CG
|
C:HIS226
|
4.0
|
15.7
|
1.0
|
CG
|
C:HIS230
|
4.0
|
9.6
|
1.0
|
ND1
|
C:HIS226
|
4.1
|
10.3
|
1.0
|
CG
|
C:HIS236
|
4.1
|
6.0
|
1.0
|
ND1
|
C:HIS236
|
4.2
|
11.0
|
1.0
|
C17
|
D:L29303
|
4.3
|
11.8
|
1.0
|
ND1
|
C:HIS230
|
4.3
|
6.8
|
1.0
|
O
|
D:HOH403
|
4.4
|
7.7
|
1.0
|
C12
|
D:L29303
|
4.6
|
5.3
|
1.0
|
C11
|
D:L29303
|
4.6
|
6.0
|
1.0
|
OE1
|
C:GLN227
|
4.7
|
11.3
|
1.0
|
C18
|
D:L29303
|
4.8
|
5.6
|
1.0
|
CA
|
C:PRO246
|
5.0
|
11.3
|
1.0
|
O
|
C:HOH413
|
5.0
|
8.0
|
1.0
|
|
Zinc binding site 6 out
of 8 in 4h82
Go back to
Zinc Binding Sites List in 4h82
Zinc binding site 6 out
of 8 in the Crystal Structure of Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor.
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 Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn302
b:13.2
occ:1.00
|
ND1
|
C:HIS203
|
2.0
|
9.9
|
1.0
|
OD2
|
C:ASP177
|
2.2
|
14.0
|
1.0
|
NE2
|
C:HIS175
|
2.5
|
8.7
|
1.0
|
NE2
|
C:HIS190
|
2.6
|
11.8
|
1.0
|
CG
|
C:ASP177
|
2.9
|
19.0
|
1.0
|
CG
|
C:HIS203
|
2.9
|
7.8
|
1.0
|
OD1
|
C:ASP177
|
3.0
|
24.8
|
1.0
|
CE1
|
C:HIS203
|
3.1
|
16.3
|
1.0
|
CB
|
C:HIS203
|
3.2
|
6.8
|
1.0
|
CD2
|
C:HIS175
|
3.2
|
14.0
|
1.0
|
CD2
|
C:HIS190
|
3.2
|
7.2
|
1.0
|
CE1
|
C:HIS175
|
3.4
|
12.1
|
1.0
|
CE1
|
C:HIS190
|
3.7
|
9.2
|
1.0
|
CD2
|
C:HIS203
|
4.1
|
6.8
|
1.0
|
O
|
C:TYR179
|
4.1
|
14.9
|
1.0
|
NE2
|
C:HIS203
|
4.1
|
14.1
|
1.0
|
CB
|
C:ASP177
|
4.2
|
17.5
|
1.0
|
CG
|
C:HIS175
|
4.3
|
14.4
|
1.0
|
ND1
|
C:HIS175
|
4.4
|
11.2
|
1.0
|
CE2
|
C:PHE181
|
4.5
|
7.5
|
1.0
|
CG
|
C:HIS190
|
4.5
|
12.0
|
1.0
|
CZ
|
C:PHE192
|
4.6
|
8.0
|
1.0
|
CZ
|
C:PHE181
|
4.6
|
11.3
|
1.0
|
ND1
|
C:HIS190
|
4.7
|
10.5
|
1.0
|
CA
|
C:HIS203
|
4.7
|
7.0
|
1.0
|
CE1
|
C:PHE192
|
4.7
|
8.0
|
1.0
|
CB
|
C:TYR179
|
4.9
|
12.9
|
1.0
|
O
|
C:HIS175
|
5.0
|
14.9
|
1.0
|
|
Zinc binding site 7 out
of 8 in 4h82
Go back to
Zinc Binding Sites List in 4h82
Zinc binding site 7 out
of 8 in the Crystal Structure of Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor.
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 Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn302
b:13.6
occ:1.00
|
NE2
|
D:HIS190
|
2.0
|
3.8
|
1.0
|
OD2
|
D:ASP177
|
2.0
|
7.5
|
1.0
|
NE2
|
D:HIS175
|
2.0
|
5.4
|
1.0
|
ND1
|
D:HIS203
|
2.0
|
7.4
|
1.0
|
CG
|
D:ASP177
|
2.8
|
9.6
|
1.0
|
CE1
|
D:HIS203
|
2.9
|
7.9
|
1.0
|
CE1
|
D:HIS190
|
2.9
|
4.5
|
1.0
|
CD2
|
D:HIS190
|
3.0
|
6.8
|
1.0
|
CE1
|
D:HIS175
|
3.0
|
5.7
|
1.0
|
CD2
|
D:HIS175
|
3.0
|
9.5
|
1.0
|
OD1
|
D:ASP177
|
3.1
|
11.3
|
1.0
|
CG
|
D:HIS203
|
3.1
|
8.3
|
1.0
|
CB
|
D:HIS203
|
3.6
|
10.8
|
1.0
|
NE2
|
D:HIS203
|
4.0
|
12.4
|
1.0
|
ND1
|
D:HIS190
|
4.1
|
7.5
|
1.0
|
CB
|
D:ASP177
|
4.1
|
7.6
|
1.0
|
ND1
|
D:HIS175
|
4.1
|
13.3
|
1.0
|
CG
|
D:HIS190
|
4.1
|
7.4
|
1.0
|
CG
|
D:HIS175
|
4.2
|
13.3
|
1.0
|
CD2
|
D:HIS203
|
4.2
|
8.4
|
1.0
|
O
|
D:TYR179
|
4.3
|
16.1
|
1.0
|
CE1
|
D:PHE192
|
4.3
|
3.4
|
1.0
|
O
|
D:HOH500
|
4.3
|
18.5
|
1.0
|
CZ
|
D:PHE192
|
4.6
|
6.8
|
1.0
|
CZ
|
D:PHE181
|
4.9
|
4.2
|
1.0
|
|
Zinc binding site 8 out
of 8 in 4h82
Go back to
Zinc Binding Sites List in 4h82
Zinc binding site 8 out
of 8 in the Crystal Structure of Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor.
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 Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn304
b:8.3
occ:1.00
|
O61
|
D:L29303
|
1.8
|
13.4
|
1.0
|
O62
|
D:L29303
|
1.9
|
14.2
|
1.0
|
NE2
|
D:HIS226
|
1.9
|
3.5
|
1.0
|
NE2
|
D:HIS230
|
2.4
|
7.8
|
1.0
|
N61
|
D:L29303
|
2.4
|
13.4
|
1.0
|
C60
|
D:L29303
|
2.5
|
14.0
|
1.0
|
NE2
|
D:HIS236
|
2.7
|
10.3
|
1.0
|
CD2
|
D:HIS226
|
2.7
|
8.8
|
1.0
|
CE1
|
D:HIS226
|
3.1
|
6.4
|
1.0
|
CD2
|
D:HIS230
|
3.1
|
4.7
|
1.0
|
CE1
|
D:HIS230
|
3.5
|
9.3
|
1.0
|
CE1
|
D:HIS236
|
3.5
|
12.9
|
1.0
|
CD2
|
D:HIS236
|
3.7
|
9.2
|
1.0
|
CG
|
D:HIS226
|
4.0
|
5.8
|
1.0
|
O
|
D:HOH402
|
4.0
|
15.4
|
1.0
|
C56
|
D:L29303
|
4.0
|
13.4
|
1.0
|
ND1
|
D:HIS226
|
4.1
|
6.1
|
1.0
|
C59
|
D:L29303
|
4.3
|
10.4
|
1.0
|
CG
|
D:HIS230
|
4.3
|
6.6
|
1.0
|
NE2
|
D:GLN227
|
4.5
|
9.8
|
1.0
|
ND1
|
D:HIS230
|
4.5
|
5.3
|
1.0
|
OE1
|
D:GLN227
|
4.5
|
9.0
|
1.0
|
C5A
|
D:L29303
|
4.6
|
7.0
|
1.0
|
C49
|
D:L29303
|
4.6
|
1.9
|
1.0
|
ND1
|
D:HIS236
|
4.7
|
3.6
|
1.0
|
C57
|
D:L29303
|
4.7
|
7.8
|
1.0
|
C39
|
D:L29303
|
4.7
|
12.9
|
1.0
|
CG
|
D:HIS236
|
4.8
|
7.6
|
1.0
|
C45
|
D:L29303
|
4.8
|
7.2
|
1.0
|
C48
|
D:L29303
|
4.8
|
7.0
|
1.0
|
N40
|
D:L29303
|
4.9
|
15.8
|
1.0
|
CD
|
D:GLN227
|
4.9
|
10.6
|
1.0
|
CB
|
D:PRO246
|
4.9
|
5.5
|
1.0
|
O
|
D:HOH415
|
5.0
|
10.7
|
1.0
|
C46
|
D:L29303
|
5.0
|
7.3
|
1.0
|
|
Reference:
C.Antoni,
L.Vera,
L.Devel,
M.P.Catalani,
B.Czarny,
E.Cassar-Lajeunesse,
E.Nuti,
A.Rossello,
V.Dive,
E.A.Stura.
Crystallization of Bi-Functional Ligand Protein Complexes. J.Struct.Biol. V. 182 246 2013.
ISSN: ISSN 1047-8477
PubMed: 23567804
DOI: 10.1016/J.JSB.2013.03.015
Page generated: Sat Oct 26 23:55:22 2024
|