Zinc in PDB 4h1q: 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: 4h1q
was solved by
E.A.Stura,
L.Vera,
E.Cassar-Lajeunesse,
E.Nuti,
M.P.Catalani,
V.Dive,
A.Rossello,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
43.09 /
1.59
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
44.140,
48.660,
67.920,
90.00,
102.55,
90.00
|
R / Rfree (%)
|
17 /
21.1
|
Other elements in 4h1q:
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 4h1q). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
Crystal Structure of Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor., PDB code: 4h1q:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 4h1q
Go back to
Zinc Binding Sites List in 4h1q
Zinc binding site 1 out
of 4 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:11.1
occ:1.00
|
NE2
|
A:HIS230
|
2.0
|
10.7
|
1.0
|
NE2
|
A:HIS236
|
2.0
|
9.6
|
1.0
|
NE2
|
A:HIS226
|
2.1
|
10.4
|
1.0
|
O25
|
A:0XX307
|
2.1
|
17.2
|
1.0
|
O23
|
A:0XX307
|
2.3
|
35.3
|
1.0
|
C21
|
A:0XX307
|
2.9
|
26.5
|
1.0
|
CD2
|
A:HIS226
|
3.0
|
11.2
|
1.0
|
CE1
|
A:HIS230
|
3.0
|
11.1
|
1.0
|
CE1
|
A:HIS236
|
3.0
|
13.7
|
1.0
|
CD2
|
A:HIS236
|
3.0
|
11.0
|
1.0
|
N22
|
A:0XX307
|
3.0
|
25.2
|
1.0
|
CD2
|
A:HIS230
|
3.1
|
13.6
|
1.0
|
CE1
|
A:HIS226
|
3.1
|
10.2
|
1.0
|
ND1
|
A:HIS236
|
4.1
|
12.0
|
1.0
|
ND1
|
A:HIS230
|
4.1
|
10.2
|
1.0
|
CG
|
A:HIS236
|
4.2
|
12.0
|
1.0
|
CG
|
A:HIS226
|
4.2
|
8.6
|
1.0
|
ND1
|
A:HIS226
|
4.2
|
8.9
|
1.0
|
CG
|
A:HIS230
|
4.2
|
11.0
|
1.0
|
C20
|
A:0XX307
|
4.4
|
18.4
|
1.0
|
N28
|
A:0XX307
|
4.4
|
16.4
|
1.0
|
C29
|
A:0XX307
|
4.5
|
20.1
|
1.0
|
O17
|
A:0XX307
|
4.5
|
31.4
|
1.0
|
C30
|
A:0XX307
|
4.5
|
17.0
|
1.0
|
OE1
|
A:GLN227
|
4.7
|
19.5
|
1.0
|
CE
|
A:MET244
|
4.8
|
7.5
|
1.0
|
C2
|
A:0XX307
|
5.0
|
18.8
|
1.0
|
N16
|
A:0XX307
|
5.0
|
23.1
|
1.0
|
|
Zinc binding site 2 out
of 4 in 4h1q
Go back to
Zinc Binding Sites List in 4h1q
Zinc binding site 2 out
of 4 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:15.1
occ:1.00
|
OD1
|
A:ASP177
|
1.9
|
20.5
|
1.0
|
NE2
|
A:HIS190
|
1.9
|
15.4
|
1.0
|
NE2
|
A:HIS175
|
1.9
|
13.6
|
1.0
|
ND1
|
A:HIS203
|
2.0
|
13.6
|
1.0
|
CE1
|
A:HIS190
|
2.8
|
18.3
|
1.0
|
CG
|
A:ASP177
|
2.9
|
21.6
|
1.0
|
CD2
|
A:HIS175
|
2.9
|
15.0
|
1.0
|
CE1
|
A:HIS175
|
3.0
|
14.2
|
1.0
|
CE1
|
A:HIS203
|
3.0
|
17.8
|
1.0
|
CG
|
A:HIS203
|
3.1
|
10.5
|
1.0
|
CD2
|
A:HIS190
|
3.1
|
12.1
|
1.0
|
OD2
|
A:ASP177
|
3.1
|
22.0
|
1.0
|
CB
|
A:HIS203
|
3.4
|
9.4
|
1.0
|
ND1
|
A:HIS190
|
3.9
|
17.5
|
1.0
|
ND1
|
A:HIS175
|
4.1
|
14.6
|
1.0
|
CG
|
A:HIS175
|
4.1
|
15.1
|
1.0
|
NE2
|
A:HIS203
|
4.1
|
12.8
|
1.0
|
CG
|
A:HIS190
|
4.1
|
10.4
|
1.0
|
CD2
|
A:HIS203
|
4.2
|
10.2
|
1.0
|
CB
|
A:ASP177
|
4.2
|
23.1
|
1.0
|
O
|
A:TYR179
|
4.3
|
17.9
|
1.0
|
CE1
|
A:PHE192
|
4.4
|
24.0
|
1.0
|
CZ
|
A:PHE181
|
4.7
|
14.3
|
1.0
|
CE2
|
A:PHE181
|
4.7
|
11.3
|
1.0
|
O
|
A:HOH489
|
4.7
|
19.9
|
1.0
|
CZ
|
A:PHE192
|
4.8
|
26.3
|
1.0
|
O
|
A:HOH475
|
4.9
|
27.4
|
1.0
|
CA
|
A:HIS203
|
4.9
|
7.3
|
1.0
|
|
Zinc binding site 3 out
of 4 in 4h1q
Go back to
Zinc Binding Sites List in 4h1q
Zinc binding site 3 out
of 4 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:Zn301
b:10.9
occ:1.00
|
NE2
|
B:HIS236
|
2.0
|
12.7
|
1.0
|
NE2
|
B:HIS230
|
2.0
|
7.5
|
1.0
|
NE2
|
B:HIS226
|
2.1
|
12.3
|
1.0
|
O25
|
B:0XX306
|
2.1
|
14.4
|
1.0
|
O23
|
B:0XX306
|
2.2
|
36.3
|
1.0
|
C21
|
B:0XX306
|
2.7
|
21.9
|
1.0
|
N22
|
B:0XX306
|
2.7
|
20.5
|
1.0
|
CD2
|
B:HIS236
|
3.0
|
10.1
|
1.0
|
CE1
|
B:HIS236
|
3.0
|
14.6
|
1.0
|
CE1
|
B:HIS230
|
3.0
|
10.9
|
1.0
|
CD2
|
B:HIS226
|
3.0
|
11.2
|
1.0
|
CD2
|
B:HIS230
|
3.0
|
7.5
|
1.0
|
CE1
|
B:HIS226
|
3.1
|
11.4
|
1.0
|
ND1
|
B:HIS236
|
4.1
|
14.5
|
1.0
|
ND1
|
B:HIS230
|
4.1
|
7.1
|
1.0
|
CG
|
B:HIS236
|
4.1
|
12.5
|
1.0
|
CG
|
B:HIS230
|
4.2
|
5.7
|
1.0
|
ND1
|
B:HIS226
|
4.2
|
7.5
|
1.0
|
CG
|
B:HIS226
|
4.2
|
8.7
|
1.0
|
C20
|
B:0XX306
|
4.3
|
14.0
|
1.0
|
C30
|
B:0XX306
|
4.5
|
19.7
|
1.0
|
O17
|
B:0XX306
|
4.5
|
29.8
|
1.0
|
C29
|
B:0XX306
|
4.5
|
24.3
|
1.0
|
N28
|
B:0XX306
|
4.6
|
24.4
|
1.0
|
OE1
|
B:GLN227
|
4.7
|
18.7
|
1.0
|
CE
|
B:MET244
|
4.9
|
8.6
|
1.0
|
N16
|
B:0XX306
|
4.9
|
18.7
|
1.0
|
C3
|
B:0XX306
|
4.9
|
17.4
|
1.0
|
C2
|
B:0XX306
|
5.0
|
14.1
|
1.0
|
|
Zinc binding site 4 out
of 4 in 4h1q
Go back to
Zinc Binding Sites List in 4h1q
Zinc binding site 4 out
of 4 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:Zn302
b:13.8
occ:1.00
|
OD1
|
B:ASP177
|
1.9
|
16.8
|
1.0
|
NE2
|
B:HIS175
|
2.0
|
11.1
|
1.0
|
NE2
|
B:HIS190
|
2.0
|
14.1
|
1.0
|
ND1
|
B:HIS203
|
2.1
|
10.4
|
1.0
|
CG
|
B:ASP177
|
2.8
|
23.6
|
1.0
|
CE1
|
B:HIS190
|
2.9
|
14.3
|
1.0
|
CD2
|
B:HIS175
|
3.0
|
16.1
|
1.0
|
CE1
|
B:HIS175
|
3.0
|
16.0
|
1.0
|
CE1
|
B:HIS203
|
3.0
|
13.4
|
1.0
|
CD2
|
B:HIS190
|
3.1
|
13.5
|
1.0
|
CG
|
B:HIS203
|
3.1
|
13.6
|
1.0
|
OD2
|
B:ASP177
|
3.2
|
23.9
|
1.0
|
CB
|
B:HIS203
|
3.5
|
9.1
|
1.0
|
ND1
|
B:HIS190
|
4.1
|
15.7
|
1.0
|
ND1
|
B:HIS175
|
4.1
|
14.4
|
1.0
|
CG
|
B:HIS175
|
4.1
|
19.2
|
1.0
|
O
|
B:TYR179
|
4.1
|
22.0
|
1.0
|
CB
|
B:ASP177
|
4.2
|
20.6
|
1.0
|
NE2
|
B:HIS203
|
4.2
|
12.1
|
1.0
|
CG
|
B:HIS190
|
4.2
|
15.3
|
1.0
|
CD2
|
B:HIS203
|
4.2
|
10.1
|
1.0
|
CE1
|
B:PHE192
|
4.5
|
18.2
|
1.0
|
CZ
|
B:PHE181
|
4.6
|
10.1
|
1.0
|
CE2
|
B:PHE181
|
4.8
|
11.7
|
1.0
|
O
|
B:HOH466
|
4.8
|
25.4
|
1.0
|
O
|
B:HOH477
|
4.9
|
25.4
|
1.0
|
CZ
|
B:PHE192
|
4.9
|
15.7
|
1.0
|
CA
|
B:HIS203
|
5.0
|
8.9
|
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 23:47:16 2024
|