Calcium 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:
Calcium Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
12;
Binding sites:
The binding sites of Calcium 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 Calcium atom.
In total 12 binding sites of Calcium where determined in the
Crystal Structure of Mutant Mmp-9 Catalytic Domain in Complex with A Twin Inhibitor., PDB code: 4h82:
Jump to Calcium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Calcium binding site 1 out
of 12 in 4h82
Go back to
Calcium Binding Sites List in 4h82
Calcium binding site 1 out
of 12 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 Calcium with other atoms in the Ca 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:Ca303
b:9.2
occ:1.00
|
OD1
|
A:ASP201
|
2.2
|
6.9
|
1.0
|
|
O
|
A:HOH439
|
2.3
|
1.4
|
1.0
|
|
O
|
A:HOH462
|
2.3
|
13.3
|
1.0
|
|
O
|
A:ASP165
|
2.3
|
19.1
|
1.0
|
|
O
|
A:GLY197
|
2.4
|
19.2
|
1.0
|
|
O
|
A:GLN199
|
2.9
|
15.3
|
1.0
|
|
CG
|
A:ASP201
|
3.2
|
12.4
|
1.0
|
|
C
|
A:GLY197
|
3.5
|
8.1
|
1.0
|
|
C
|
A:ASP165
|
3.5
|
13.1
|
1.0
|
|
OD2
|
A:ASP201
|
3.7
|
14.7
|
1.0
|
|
C
|
A:GLN199
|
3.8
|
16.0
|
1.0
|
|
O
|
A:HOH493
|
4.0
|
9.3
|
1.0
|
|
N
|
A:ASP201
|
4.0
|
10.6
|
1.0
|
|
O
|
A:ALA164
|
4.1
|
10.0
|
1.0
|
|
C
|
A:ILE198
|
4.1
|
9.6
|
1.0
|
|
N
|
A:VAL167
|
4.1
|
13.3
|
1.0
|
|
O
|
A:ILE198
|
4.3
|
14.8
|
1.0
|
|
N
|
A:ILE198
|
4.3
|
19.9
|
1.0
|
|
CA
|
A:ILE198
|
4.3
|
7.4
|
1.0
|
|
N
|
A:GLN199
|
4.3
|
10.1
|
1.0
|
|
O
|
A:HOH480
|
4.3
|
22.0
|
1.0
|
|
CA
|
A:GLY200
|
4.4
|
4.7
|
1.0
|
|
N
|
A:GLY200
|
4.4
|
8.7
|
1.0
|
|
C
|
A:GLY200
|
4.4
|
6.6
|
1.0
|
|
CA
|
A:ASP165
|
4.4
|
10.2
|
1.0
|
|
CB
|
A:ASP201
|
4.5
|
8.2
|
1.0
|
|
N
|
A:ILE166
|
4.5
|
12.2
|
1.0
|
|
CA
|
A:GLY197
|
4.5
|
10.2
|
1.0
|
|
CA
|
A:ILE166
|
4.5
|
8.5
|
1.0
|
|
CG2
|
A:VAL167
|
4.5
|
2.9
|
1.0
|
|
CA
|
A:ASP201
|
4.5
|
6.7
|
1.0
|
|
N
|
A:GLY197
|
4.6
|
6.4
|
1.0
|
|
O
|
A:GLY195
|
4.6
|
10.4
|
1.0
|
|
CA
|
A:GLN199
|
4.7
|
12.1
|
1.0
|
|
CB
|
A:VAL167
|
4.7
|
8.7
|
1.0
|
|
C
|
A:ILE166
|
4.8
|
9.6
|
1.0
|
|
Calcium binding site 2 out
of 12 in 4h82
Go back to
Calcium Binding Sites List in 4h82
Calcium binding site 2 out
of 12 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 Calcium with other atoms in the Ca 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:Ca304
b:25.0
occ:1.00
|
OD1
|
A:ASP182
|
2.2
|
24.4
|
1.0
|
|
O
|
A:LEU187
|
2.3
|
20.9
|
1.0
|
|
OE2
|
A:GLU208
|
2.3
|
17.4
|
1.0
|
|
O
|
A:ASP185
|
2.5
|
31.6
|
1.0
|
|
O
|
A:GLY183
|
2.7
|
28.2
|
1.0
|
|
OD2
|
A:ASP205
|
2.8
|
17.2
|
1.0
|
|
C
|
A:LEU187
|
3.2
|
21.3
|
1.0
|
|
N
|
A:LEU187
|
3.4
|
16.5
|
1.0
|
|
CG
|
A:ASP182
|
3.4
|
14.3
|
1.0
|
|
CD
|
A:GLU208
|
3.5
|
17.1
|
1.0
|
|
C
|
A:ASP185
|
3.5
|
25.1
|
1.0
|
|
CA
|
A:LEU187
|
3.6
|
20.8
|
1.0
|
|
CB
|
A:LEU187
|
3.7
|
24.0
|
1.0
|
|
CG
|
A:ASP205
|
3.7
|
12.0
|
1.0
|
|
C
|
A:GLY183
|
3.8
|
11.1
|
1.0
|
|
O
|
A:HOH502
|
4.1
|
20.8
|
1.0
|
|
OD2
|
A:ASP182
|
4.1
|
14.6
|
1.0
|
|
N
|
A:GLY183
|
4.1
|
18.9
|
1.0
|
|
N
|
A:ASP182
|
4.1
|
22.1
|
1.0
|
|
C
|
A:GLY186
|
4.1
|
17.2
|
1.0
|
|
CB
|
A:ASP205
|
4.2
|
17.6
|
1.0
|
|
C
|
A:ASP182
|
4.2
|
17.2
|
1.0
|
|
N
|
A:GLY186
|
4.3
|
25.1
|
1.0
|
|
N
|
A:ASP185
|
4.3
|
16.9
|
1.0
|
|
OE1
|
A:GLU208
|
4.4
|
21.8
|
1.0
|
|
CA
|
A:GLY186
|
4.4
|
23.4
|
1.0
|
|
CG
|
A:GLU208
|
4.4
|
7.3
|
1.0
|
|
N
|
A:LEU188
|
4.5
|
15.4
|
1.0
|
|
C
|
A:LYS184
|
4.5
|
23.9
|
1.0
|
|
CA
|
A:ASP182
|
4.5
|
14.3
|
1.0
|
|
CA
|
A:ASP185
|
4.5
|
28.3
|
1.0
|
|
CA
|
A:GLY183
|
4.5
|
13.2
|
1.0
|
|
CB
|
A:ASP182
|
4.6
|
9.1
|
1.0
|
|
O
|
A:LYS184
|
4.7
|
30.7
|
1.0
|
|
OD1
|
A:ASP205
|
4.7
|
10.5
|
1.0
|
|
O
|
A:ASP182
|
4.7
|
34.4
|
1.0
|
|
N
|
A:LYS184
|
4.8
|
26.5
|
1.0
|
|
CB
|
A:PHE181
|
4.9
|
24.1
|
1.0
|
|
CG
|
A:LEU187
|
4.9
|
17.5
|
1.0
|
|
CA
|
A:LEU188
|
4.9
|
11.9
|
1.0
|
|
Calcium binding site 3 out
of 12 in 4h82
Go back to
Calcium Binding Sites List in 4h82
Calcium binding site 3 out
of 12 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 Calcium with other atoms in the Ca 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
|
A:Ca305
b:39.4
occ:1.00
|
OD2
|
A:ASP131
|
2.5
|
14.8
|
1.0
|
|
O
|
A:ASP206
|
2.5
|
18.0
|
1.0
|
|
O
|
A:GLU208
|
2.6
|
22.7
|
1.0
|
|
O
|
A:HOH428
|
2.7
|
14.1
|
1.0
|
|
OD1
|
A:ASP206
|
3.1
|
22.0
|
1.0
|
|
CG
|
A:ASP131
|
3.3
|
21.3
|
1.0
|
|
C
|
A:ASP206
|
3.3
|
13.1
|
1.0
|
|
OD1
|
A:ASP131
|
3.4
|
19.9
|
1.0
|
|
C
|
A:GLU208
|
3.6
|
18.9
|
1.0
|
|
CA
|
A:ASP206
|
3.7
|
9.8
|
1.0
|
|
OG
|
A:SER129
|
3.9
|
13.2
|
1.0
|
|
CD1
|
A:TRP210
|
3.9
|
13.1
|
1.0
|
|
CG
|
A:ASP206
|
4.0
|
6.9
|
1.0
|
|
CA
|
A:LEU209
|
4.1
|
16.3
|
1.0
|
|
N
|
A:LEU209
|
4.2
|
22.5
|
1.0
|
|
N
|
A:GLU208
|
4.3
|
18.4
|
1.0
|
|
N
|
A:ASP207
|
4.3
|
14.3
|
1.0
|
|
N
|
A:TRP210
|
4.3
|
18.8
|
1.0
|
|
CB
|
A:ASP206
|
4.4
|
8.2
|
1.0
|
|
C
|
A:ASP207
|
4.4
|
11.7
|
1.0
|
|
CA
|
A:GLU208
|
4.6
|
15.5
|
1.0
|
|
CA
|
A:ASP207
|
4.6
|
14.2
|
1.0
|
|
O
|
A:ASP205
|
4.7
|
15.7
|
1.0
|
|
NE1
|
A:TRP210
|
4.7
|
7.6
|
1.0
|
|
C
|
A:LEU209
|
4.7
|
15.0
|
1.0
|
|
CB
|
A:ASP131
|
4.7
|
14.1
|
1.0
|
|
CG
|
A:TRP210
|
4.8
|
13.1
|
1.0
|
|
O
|
A:ASP207
|
4.8
|
11.5
|
1.0
|
|
CB
|
A:SER129
|
5.0
|
16.6
|
1.0
|
|
N
|
A:ASP206
|
5.0
|
10.7
|
1.0
|
|
Calcium binding site 4 out
of 12 in 4h82
Go back to
Calcium Binding Sites List in 4h82
Calcium binding site 4 out
of 12 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 Calcium with other atoms in the Ca 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:Ca302
b:4.4
occ:1.00
|
O
|
B:ASP165
|
2.2
|
10.8
|
1.0
|
|
O
|
B:HOH437
|
2.4
|
7.9
|
1.0
|
|
OD1
|
B:ASP201
|
2.4
|
6.4
|
1.0
|
|
O
|
B:GLN199
|
2.4
|
6.2
|
1.0
|
|
O
|
B:HOH567
|
2.4
|
7.5
|
1.0
|
|
O
|
B:GLY197
|
2.4
|
17.2
|
1.0
|
|
C
|
B:ASP165
|
3.4
|
8.1
|
1.0
|
|
C
|
B:GLY197
|
3.5
|
11.1
|
1.0
|
|
CG
|
B:ASP201
|
3.5
|
9.3
|
1.0
|
|
C
|
B:GLN199
|
3.6
|
3.0
|
1.0
|
|
N
|
B:ASP201
|
4.0
|
8.8
|
1.0
|
|
O
|
B:ALA164
|
4.2
|
15.1
|
1.0
|
|
O
|
B:HOH438
|
4.2
|
8.8
|
1.0
|
|
C
|
B:ILE198
|
4.2
|
13.0
|
1.0
|
|
OD2
|
B:ASP201
|
4.2
|
4.4
|
1.0
|
|
CA
|
B:ASP165
|
4.2
|
10.9
|
1.0
|
|
CA
|
B:GLY200
|
4.2
|
4.5
|
1.0
|
|
C
|
B:GLY200
|
4.3
|
5.8
|
1.0
|
|
N
|
B:ILE166
|
4.3
|
7.2
|
1.0
|
|
N
|
B:GLN199
|
4.3
|
9.3
|
1.0
|
|
O
|
B:ILE198
|
4.3
|
9.1
|
1.0
|
|
N
|
B:GLY200
|
4.4
|
4.4
|
1.0
|
|
CA
|
B:GLY197
|
4.4
|
7.2
|
1.0
|
|
CA
|
B:ILE166
|
4.4
|
7.3
|
1.0
|
|
N
|
B:ILE198
|
4.4
|
17.4
|
1.0
|
|
N
|
B:GLY197
|
4.4
|
10.6
|
1.0
|
|
O
|
B:GLY195
|
4.4
|
11.0
|
1.0
|
|
CA
|
B:ILE198
|
4.5
|
18.1
|
1.0
|
|
N
|
B:VAL167
|
4.5
|
6.7
|
1.0
|
|
CA
|
B:GLN199
|
4.6
|
7.6
|
1.0
|
|
CB
|
B:ASP201
|
4.6
|
6.7
|
1.0
|
|
CA
|
B:ASP201
|
4.6
|
6.2
|
1.0
|
|
C
|
B:PRO196
|
4.7
|
6.9
|
1.0
|
|
O
|
B:PRO196
|
4.8
|
9.8
|
1.0
|
|
CG2
|
B:VAL167
|
4.8
|
4.6
|
1.0
|
|
O
|
B:HOH440
|
4.9
|
18.9
|
1.0
|
|
CH2
|
B:TRP116
|
4.9
|
12.5
|
1.0
|
|
C
|
B:ILE166
|
4.9
|
5.8
|
1.0
|
|
O
|
B:GLY200
|
5.0
|
7.4
|
1.0
|
|
Calcium binding site 5 out
of 12 in 4h82
Go back to
Calcium Binding Sites List in 4h82
Calcium binding site 5 out
of 12 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 Calcium with other atoms in the Ca 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
|
B:Ca303
b:12.7
occ:1.00
|
OE2
|
B:GLU208
|
2.2
|
8.8
|
1.0
|
|
O
|
B:GLY183
|
2.2
|
18.2
|
1.0
|
|
O
|
B:ASP185
|
2.4
|
31.5
|
1.0
|
|
OD2
|
B:ASP205
|
2.4
|
18.0
|
1.0
|
|
O
|
B:LEU187
|
2.5
|
11.7
|
1.0
|
|
OD1
|
B:ASP182
|
2.6
|
18.2
|
1.0
|
|
CD
|
B:GLU208
|
3.2
|
19.2
|
1.0
|
|
CG
|
B:ASP205
|
3.2
|
12.6
|
1.0
|
|
C
|
B:GLY183
|
3.4
|
17.7
|
1.0
|
|
C
|
B:ASP185
|
3.5
|
21.0
|
1.0
|
|
C
|
B:LEU187
|
3.6
|
13.3
|
1.0
|
|
N
|
B:ASP185
|
3.6
|
27.9
|
1.0
|
|
C
|
B:LYS184
|
3.7
|
17.7
|
1.0
|
|
CG
|
B:ASP182
|
3.8
|
12.1
|
1.0
|
|
OD1
|
B:ASP205
|
3.9
|
12.0
|
1.0
|
|
CG
|
B:GLU208
|
3.9
|
9.7
|
1.0
|
|
OE1
|
B:GLU208
|
4.0
|
7.7
|
1.0
|
|
N
|
B:LEU187
|
4.0
|
11.7
|
1.0
|
|
CA
|
B:LYS184
|
4.0
|
17.1
|
1.0
|
|
CB
|
B:ASP205
|
4.1
|
15.7
|
1.0
|
|
CA
|
B:ASP185
|
4.1
|
18.2
|
1.0
|
|
N
|
B:LYS184
|
4.2
|
14.5
|
1.0
|
|
O
|
B:LYS184
|
4.2
|
19.3
|
1.0
|
|
CA
|
B:LEU187
|
4.2
|
9.8
|
1.0
|
|
N
|
B:GLY183
|
4.3
|
12.3
|
1.0
|
|
C
|
B:ASP182
|
4.3
|
18.6
|
1.0
|
|
OD2
|
B:ASP182
|
4.4
|
7.5
|
1.0
|
|
CB
|
B:LEU187
|
4.4
|
11.1
|
1.0
|
|
CA
|
B:GLY183
|
4.5
|
14.4
|
1.0
|
|
N
|
B:ASP182
|
4.5
|
25.6
|
1.0
|
|
O
|
B:ASP182
|
4.5
|
25.7
|
1.0
|
|
C
|
B:GLY186
|
4.5
|
17.3
|
1.0
|
|
N
|
B:GLY186
|
4.6
|
14.6
|
1.0
|
|
N
|
B:LEU188
|
4.7
|
6.0
|
1.0
|
|
CA
|
B:ASP182
|
4.8
|
12.4
|
1.0
|
|
CA
|
B:GLY186
|
4.9
|
21.6
|
1.0
|
|
CB
|
B:ASP182
|
4.9
|
11.9
|
1.0
|
|
CA
|
B:LEU188
|
5.0
|
11.0
|
1.0
|
|
Calcium binding site 6 out
of 12 in 4h82
Go back to
Calcium Binding Sites List in 4h82
Calcium binding site 6 out
of 12 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 Calcium with other atoms in the Ca 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
|
B:Ca304
b:36.0
occ:1.00
|
O
|
B:HOH419
|
2.3
|
11.3
|
1.0
|
|
OD2
|
B:ASP131
|
2.6
|
13.6
|
1.0
|
|
OD1
|
B:ASP131
|
2.7
|
13.2
|
1.0
|
|
O
|
B:ASP206
|
2.8
|
14.1
|
1.0
|
|
OD1
|
B:ASP206
|
2.9
|
8.8
|
1.0
|
|
CG
|
B:ASP131
|
3.0
|
13.4
|
1.0
|
|
O
|
B:GLU208
|
3.4
|
14.2
|
1.0
|
|
CG
|
B:ASP206
|
3.8
|
12.8
|
1.0
|
|
C
|
B:ASP206
|
3.9
|
13.4
|
1.0
|
|
OG
|
B:SER129
|
4.0
|
12.2
|
1.0
|
|
C
|
B:GLU208
|
4.1
|
11.2
|
1.0
|
|
O
|
B:HOH530
|
4.2
|
13.0
|
1.0
|
|
O
|
B:HOH529
|
4.3
|
14.4
|
1.0
|
|
OD2
|
B:ASP206
|
4.4
|
12.9
|
1.0
|
|
CA
|
B:LEU209
|
4.4
|
15.0
|
1.0
|
|
CB
|
B:ASP131
|
4.4
|
10.8
|
1.0
|
|
N
|
B:LEU209
|
4.5
|
10.3
|
1.0
|
|
N
|
B:GLU208
|
4.5
|
20.2
|
1.0
|
|
CA
|
B:ASP206
|
4.6
|
9.3
|
1.0
|
|
O
|
B:HOH528
|
4.7
|
16.9
|
1.0
|
|
CB
|
B:ASP206
|
4.7
|
7.8
|
1.0
|
|
C
|
B:ASP207
|
4.9
|
13.8
|
1.0
|
|
O
|
B:HOH420
|
4.9
|
9.7
|
1.0
|
|
N
|
B:ASP207
|
4.9
|
13.3
|
1.0
|
|
CD1
|
B:TRP210
|
5.0
|
9.1
|
1.0
|
|
N
|
B:TRP210
|
5.0
|
14.4
|
1.0
|
|
CA
|
B:ASP207
|
5.0
|
16.3
|
1.0
|
|
CA
|
B:GLU208
|
5.0
|
13.0
|
1.0
|
|
Calcium binding site 7 out
of 12 in 4h82
Go back to
Calcium Binding Sites List in 4h82
Calcium binding site 7 out
of 12 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 Calcium with other atoms in the Ca 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
|
C:Ca303
b:8.1
occ:1.00
|
O
|
C:ASP165
|
2.1
|
7.4
|
1.0
|
|
O
|
C:GLN199
|
2.3
|
10.9
|
1.0
|
|
O
|
C:GLY197
|
2.4
|
15.7
|
1.0
|
|
O
|
C:HOH447
|
2.4
|
18.1
|
1.0
|
|
O
|
C:HOH415
|
2.4
|
8.9
|
1.0
|
|
OD1
|
C:ASP201
|
2.5
|
9.9
|
1.0
|
|
C
|
C:ASP165
|
3.3
|
11.1
|
1.0
|
|
C
|
C:GLN199
|
3.4
|
6.9
|
1.0
|
|
C
|
C:GLY197
|
3.5
|
11.6
|
1.0
|
|
CG
|
C:ASP201
|
3.7
|
13.7
|
1.0
|
|
N
|
C:GLY197
|
4.0
|
7.5
|
1.0
|
|
N
|
C:ASP201
|
4.0
|
9.1
|
1.0
|
|
CA
|
C:GLY200
|
4.1
|
10.7
|
1.0
|
|
C
|
C:GLY200
|
4.1
|
6.3
|
1.0
|
|
O
|
C:HOH464
|
4.1
|
17.1
|
1.0
|
|
O
|
C:ALA164
|
4.1
|
19.2
|
1.0
|
|
CA
|
C:ASP165
|
4.2
|
10.6
|
1.0
|
|
CA
|
C:GLY197
|
4.2
|
16.5
|
1.0
|
|
N
|
C:GLY200
|
4.2
|
7.4
|
1.0
|
|
N
|
C:GLN199
|
4.2
|
13.6
|
1.0
|
|
N
|
C:ILE166
|
4.3
|
17.1
|
1.0
|
|
C
|
C:ILE198
|
4.3
|
14.1
|
1.0
|
|
OD2
|
C:ASP201
|
4.4
|
8.8
|
1.0
|
|
C
|
C:PRO196
|
4.4
|
9.6
|
1.0
|
|
CA
|
C:ILE166
|
4.5
|
7.4
|
1.0
|
|
O
|
C:GLY195
|
4.5
|
8.8
|
1.0
|
|
CA
|
C:GLN199
|
4.5
|
8.6
|
1.0
|
|
N
|
C:ILE198
|
4.5
|
11.6
|
1.0
|
|
O
|
C:HOH471
|
4.5
|
12.5
|
1.0
|
|
O
|
C:ILE198
|
4.6
|
13.9
|
1.0
|
|
CB
|
C:ASP201
|
4.7
|
11.1
|
1.0
|
|
CA
|
C:ASP201
|
4.7
|
7.5
|
1.0
|
|
O
|
C:GLY200
|
4.7
|
11.4
|
1.0
|
|
CH2
|
C:TRP116
|
4.7
|
4.4
|
1.0
|
|
N
|
C:VAL167
|
4.8
|
8.2
|
1.0
|
|
CA
|
C:ILE198
|
4.8
|
9.2
|
1.0
|
|
CG2
|
C:VAL167
|
4.8
|
10.9
|
1.0
|
|
CA
|
C:PRO196
|
4.9
|
7.6
|
1.0
|
|
O
|
C:PRO196
|
5.0
|
19.8
|
1.0
|
|
Calcium binding site 8 out
of 12 in 4h82
Go back to
Calcium Binding Sites List in 4h82
Calcium binding site 8 out
of 12 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 Calcium with other atoms in the Ca 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
|
C:Ca304
b:10.9
occ:1.00
|
O
|
C:LEU187
|
2.3
|
8.2
|
1.0
|
|
O
|
C:GLY183
|
2.3
|
15.8
|
1.0
|
|
OD2
|
C:ASP205
|
2.4
|
15.1
|
1.0
|
|
O
|
C:ASP185
|
2.5
|
13.6
|
1.0
|
|
OD1
|
C:ASP182
|
2.5
|
23.2
|
1.0
|
|
OE2
|
C:GLU208
|
2.8
|
23.9
|
1.0
|
|
C
|
C:LEU187
|
3.4
|
15.2
|
1.0
|
|
C
|
C:GLY183
|
3.5
|
20.0
|
1.0
|
|
CG
|
C:ASP205
|
3.5
|
9.7
|
1.0
|
|
C
|
C:ASP185
|
3.7
|
15.8
|
1.0
|
|
CD
|
C:GLU208
|
3.7
|
11.8
|
1.0
|
|
CG
|
C:ASP182
|
3.7
|
11.9
|
1.0
|
|
CG
|
C:GLU208
|
3.9
|
10.4
|
1.0
|
|
N
|
C:GLY183
|
4.0
|
16.5
|
1.0
|
|
N
|
C:LEU187
|
4.0
|
12.4
|
1.0
|
|
CB
|
C:ASP205
|
4.0
|
15.0
|
1.0
|
|
N
|
C:ASP185
|
4.1
|
22.3
|
1.0
|
|
N
|
C:ASP182
|
4.1
|
14.0
|
1.0
|
|
C
|
C:ASP182
|
4.2
|
11.7
|
1.0
|
|
CA
|
C:LEU187
|
4.2
|
14.4
|
1.0
|
|
C
|
C:LYS184
|
4.2
|
22.1
|
1.0
|
|
C
|
C:GLY186
|
4.3
|
9.7
|
1.0
|
|
CA
|
C:GLY183
|
4.3
|
17.2
|
1.0
|
|
N
|
C:LEU188
|
4.5
|
10.1
|
1.0
|
|
OD2
|
C:ASP182
|
4.5
|
13.5
|
1.0
|
|
N
|
C:LYS184
|
4.5
|
14.6
|
1.0
|
|
CA
|
C:ASP185
|
4.5
|
23.9
|
1.0
|
|
CA
|
C:LYS184
|
4.5
|
14.3
|
1.0
|
|
CA
|
C:ASP182
|
4.5
|
9.3
|
1.0
|
|
O
|
C:ASP182
|
4.6
|
16.7
|
1.0
|
|
OD1
|
C:ASP205
|
4.6
|
10.8
|
1.0
|
|
CA
|
C:LEU188
|
4.6
|
8.8
|
1.0
|
|
N
|
C:GLY186
|
4.6
|
23.7
|
1.0
|
|
CB
|
C:LEU187
|
4.6
|
9.4
|
1.0
|
|
O
|
C:LYS184
|
4.7
|
30.4
|
1.0
|
|
CB
|
C:ASP182
|
4.7
|
5.6
|
1.0
|
|
O
|
C:GLY186
|
4.8
|
11.9
|
1.0
|
|
CA
|
C:GLY186
|
4.8
|
23.6
|
1.0
|
|
OE1
|
C:GLU208
|
4.8
|
14.0
|
1.0
|
|
CD2
|
C:LEU188
|
4.9
|
14.1
|
1.0
|
|
Calcium binding site 9 out
of 12 in 4h82
Go back to
Calcium Binding Sites List in 4h82
Calcium binding site 9 out
of 12 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 Calcium with other atoms in the Ca binding
site number 9 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:Ca305
b:27.6
occ:1.00
|
OD2
|
C:ASP131
|
2.0
|
9.6
|
1.0
|
|
O
|
C:GLU208
|
2.2
|
14.7
|
1.0
|
|
O
|
C:ASP206
|
2.2
|
18.1
|
1.0
|
|
OD1
|
C:ASP206
|
2.4
|
18.4
|
1.0
|
|
CG
|
C:ASP131
|
2.9
|
12.1
|
1.0
|
|
OD1
|
C:ASP131
|
3.1
|
17.0
|
1.0
|
|
C
|
C:ASP206
|
3.2
|
19.4
|
1.0
|
|
O
|
C:HOH466
|
3.3
|
10.1
|
1.0
|
|
C
|
C:GLU208
|
3.4
|
15.8
|
1.0
|
|
CG
|
C:ASP206
|
3.5
|
20.4
|
1.0
|
|
OG
|
C:SER129
|
3.6
|
31.5
|
1.0
|
|
CA
|
C:ASP206
|
3.6
|
10.1
|
1.0
|
|
CD1
|
C:TRP210
|
3.7
|
12.9
|
1.0
|
|
CA
|
C:LEU209
|
4.0
|
18.0
|
1.0
|
|
N
|
C:LEU209
|
4.1
|
19.0
|
1.0
|
|
CB
|
C:ASP206
|
4.1
|
12.1
|
1.0
|
|
NE1
|
C:TRP210
|
4.2
|
5.7
|
1.0
|
|
N
|
C:TRP210
|
4.2
|
16.9
|
1.0
|
|
N
|
C:GLU208
|
4.3
|
22.7
|
1.0
|
|
CB
|
C:ASP131
|
4.3
|
15.7
|
1.0
|
|
OD2
|
C:ASP206
|
4.4
|
27.7
|
1.0
|
|
N
|
C:ASP207
|
4.4
|
19.6
|
1.0
|
|
CA
|
C:GLU208
|
4.4
|
15.1
|
1.0
|
|
C
|
C:ASP207
|
4.6
|
19.2
|
1.0
|
|
CB
|
C:SER129
|
4.6
|
15.5
|
1.0
|
|
C
|
C:LEU209
|
4.6
|
11.8
|
1.0
|
|
CG
|
C:TRP210
|
4.6
|
5.0
|
1.0
|
|
O
|
C:ASP205
|
4.7
|
15.7
|
1.0
|
|
CA
|
C:ASP207
|
4.8
|
15.1
|
1.0
|
|
N
|
C:ASP206
|
4.9
|
16.4
|
1.0
|
|
Calcium binding site 10 out
of 12 in 4h82
Go back to
Calcium Binding Sites List in 4h82
Calcium binding site 10 out
of 12 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 Calcium with other atoms in the Ca binding
site number 10 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:Ca305
b:15.2
occ:1.00
|
O
|
D:LEU187
|
2.2
|
21.0
|
1.0
|
|
O
|
D:ASP185
|
2.2
|
18.4
|
1.0
|
|
OD2
|
D:ASP205
|
2.3
|
14.3
|
1.0
|
|
OD1
|
D:ASP182
|
2.3
|
20.5
|
1.0
|
|
O
|
D:GLY183
|
2.4
|
25.3
|
1.0
|
|
OE2
|
D:GLU208
|
2.7
|
17.3
|
1.0
|
|
C
|
D:LEU187
|
3.2
|
11.2
|
1.0
|
|
C
|
D:ASP185
|
3.4
|
18.6
|
1.0
|
|
N
|
D:LEU187
|
3.4
|
27.7
|
1.0
|
|
CG
|
D:ASP182
|
3.4
|
24.0
|
1.0
|
|
CG
|
D:ASP205
|
3.5
|
10.7
|
1.0
|
|
C
|
D:GLY183
|
3.6
|
17.2
|
1.0
|
|
C
|
D:GLY186
|
3.7
|
16.5
|
1.0
|
|
CA
|
D:LEU187
|
3.8
|
16.6
|
1.0
|
|
CD
|
D:GLU208
|
3.8
|
14.3
|
1.0
|
|
OD2
|
D:ASP182
|
3.9
|
18.6
|
1.0
|
|
N
|
D:GLY183
|
4.0
|
11.3
|
1.0
|
|
CB
|
D:LEU187
|
4.1
|
16.1
|
1.0
|
|
N
|
D:ASP185
|
4.2
|
17.1
|
1.0
|
|
CA
|
D:GLY186
|
4.2
|
21.0
|
1.0
|
|
N
|
D:GLY186
|
4.2
|
18.9
|
1.0
|
|
C
|
D:LYS184
|
4.2
|
15.8
|
1.0
|
|
CB
|
D:ASP205
|
4.2
|
9.5
|
1.0
|
|
O
|
D:GLY186
|
4.3
|
19.0
|
1.0
|
|
CA
|
D:ASP185
|
4.3
|
16.3
|
1.0
|
|
N
|
D:LEU188
|
4.3
|
11.0
|
1.0
|
|
OD1
|
D:ASP205
|
4.4
|
9.8
|
1.0
|
|
CA
|
D:GLY183
|
4.4
|
18.0
|
1.0
|
|
O
|
D:LYS184
|
4.5
|
31.9
|
1.0
|
|
C
|
D:ASP182
|
4.5
|
12.8
|
1.0
|
|
O
|
D:HOH470
|
4.5
|
15.0
|
1.0
|
|
N
|
D:ASP182
|
4.5
|
21.1
|
1.0
|
|
CG
|
D:GLU208
|
4.5
|
8.1
|
1.0
|
|
N
|
D:LYS184
|
4.5
|
11.3
|
1.0
|
|
OE1
|
D:GLU208
|
4.6
|
12.4
|
1.0
|
|
CB
|
D:ASP182
|
4.7
|
19.1
|
1.0
|
|
CA
|
D:LYS184
|
4.7
|
12.1
|
1.0
|
|
CA
|
D:ASP182
|
4.7
|
12.4
|
1.0
|
|
CA
|
D:LEU188
|
4.8
|
7.8
|
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: Sun Jul 14 07:42:17 2024
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