Calcium in PDB 5lab: Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor Nngh
Enzymatic activity of Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor Nngh
All present enzymatic activity of Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor Nngh:
3.4.24.65;
Protein crystallography data
The structure of Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor Nngh, PDB code: 5lab
was solved by
E.Ravera,
V.Calderone,
C.Luchinat,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
20.00 /
1.34
|
Space group
|
P 21 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
69.190,
62.560,
37.260,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
15.5 /
19.5
|
Other elements in 5lab:
The structure of Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor Nngh also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor Nngh
(pdb code 5lab). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the
Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor Nngh, PDB code: 5lab:
Jump to Calcium binding site number:
1;
2;
3;
Calcium binding site 1 out
of 3 in 5lab
Go back to
Calcium Binding Sites List in 5lab
Calcium binding site 1 out
of 3 in the Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor Nngh
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 the Catalytic Domain of Human MMP12 Complexed with the Inhibitor Nngh within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca303
b:16.2
occ:1.00
|
O
|
A:GLY192
|
2.3
|
15.5
|
1.0
|
O
|
A:GLY190
|
2.3
|
18.0
|
1.0
|
O
|
A:HOH413
|
2.3
|
20.6
|
1.0
|
O
|
A:ASP158
|
2.3
|
15.1
|
1.0
|
O
|
A:HOH452
|
2.3
|
17.7
|
1.0
|
OD2
|
A:ASP194
|
2.4
|
14.6
|
1.0
|
CG
|
A:ASP194
|
3.4
|
13.3
|
1.0
|
C
|
A:ASP158
|
3.5
|
15.1
|
1.0
|
C
|
A:GLY192
|
3.5
|
15.4
|
1.0
|
C
|
A:GLY190
|
3.5
|
18.1
|
1.0
|
OD1
|
A:ASP194
|
3.8
|
15.1
|
1.0
|
C
|
A:ILE191
|
4.0
|
16.4
|
1.0
|
N
|
A:GLY192
|
4.1
|
15.8
|
1.0
|
O
|
A:ILE191
|
4.2
|
15.4
|
1.0
|
O
|
A:ALA157
|
4.2
|
17.7
|
1.0
|
N
|
A:ASP194
|
4.3
|
12.3
|
1.0
|
CA
|
A:ASP158
|
4.3
|
15.2
|
1.0
|
CA
|
A:GLY192
|
4.3
|
16.1
|
1.0
|
O
|
A:GLY188
|
4.4
|
19.3
|
1.0
|
CA
|
A:ILE191
|
4.4
|
17.7
|
1.0
|
N
|
A:ILE191
|
4.4
|
16.2
|
1.0
|
N
|
A:GLY190
|
4.4
|
20.0
|
1.0
|
CA
|
A:GLY190
|
4.4
|
18.4
|
1.0
|
N
|
A:ILE159
|
4.4
|
14.1
|
1.0
|
N
|
A:GLY193
|
4.4
|
14.8
|
1.0
|
CA
|
A:GLY193
|
4.5
|
14.6
|
1.0
|
CA
|
A:ILE159
|
4.6
|
13.9
|
1.0
|
C
|
A:GLY193
|
4.6
|
13.3
|
1.0
|
N
|
A:LEU160
|
4.6
|
13.4
|
1.0
|
O
|
A:HOH457
|
4.6
|
29.1
|
1.0
|
CB
|
A:ASP194
|
4.7
|
13.2
|
1.0
|
C
|
A:SER189
|
4.8
|
20.5
|
1.0
|
O
|
A:HOH425
|
4.8
|
22.4
|
1.0
|
CA
|
A:ASP194
|
4.8
|
12.3
|
1.0
|
CH2
|
A:TRP109
|
4.9
|
19.4
|
1.0
|
O
|
A:SER189
|
5.0
|
20.6
|
1.0
|
|
Calcium binding site 2 out
of 3 in 5lab
Go back to
Calcium Binding Sites List in 5lab
Calcium binding site 2 out
of 3 in the Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor Nngh
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 the Catalytic Domain of Human MMP12 Complexed with the Inhibitor Nngh within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca304
b:21.6
occ:1.00
|
O
|
A:HOH525
|
2.3
|
26.7
|
1.0
|
O
|
A:HOH541
|
2.3
|
26.0
|
1.0
|
O
|
A:GLU199
|
2.4
|
20.9
|
1.0
|
OD2
|
A:ASP124
|
2.4
|
23.1
|
1.0
|
O
|
A:GLU201
|
2.4
|
19.5
|
1.0
|
OE2
|
A:GLU199
|
2.4
|
19.0
|
1.0
|
OD1
|
A:ASP124
|
2.4
|
22.9
|
1.0
|
CG
|
A:ASP124
|
2.8
|
21.9
|
1.0
|
CD
|
A:GLU199
|
3.5
|
17.0
|
1.0
|
C
|
A:GLU199
|
3.5
|
17.9
|
1.0
|
C
|
A:GLU201
|
3.6
|
20.0
|
1.0
|
CG
|
A:GLU199
|
3.9
|
17.2
|
1.0
|
CA
|
A:GLU199
|
4.1
|
17.0
|
1.0
|
OG1
|
A:THR122
|
4.2
|
19.5
|
1.0
|
CA
|
A:PHE202
|
4.2
|
21.6
|
1.0
|
CB
|
A:ASP124
|
4.3
|
22.3
|
1.0
|
N
|
A:PHE202
|
4.3
|
21.8
|
1.0
|
CD1
|
A:TRP203
|
4.3
|
17.0
|
1.0
|
N
|
A:GLU201
|
4.5
|
17.4
|
1.0
|
O
|
A:HOH582
|
4.5
|
34.6
|
1.0
|
O
|
A:HOH633
|
4.5
|
39.2
|
1.0
|
C
|
A:ASP200
|
4.6
|
19.2
|
1.0
|
N
|
A:ASP200
|
4.6
|
17.4
|
1.0
|
OE1
|
A:GLU199
|
4.6
|
19.1
|
1.0
|
CB
|
A:GLU199
|
4.6
|
15.4
|
1.0
|
O
|
A:HOH501
|
4.6
|
30.0
|
1.0
|
CA
|
A:GLU201
|
4.7
|
19.0
|
1.0
|
O
|
A:HOH420
|
4.7
|
34.1
|
1.0
|
O
|
A:HOH458
|
4.7
|
33.1
|
1.0
|
CA
|
A:ASP200
|
4.7
|
18.1
|
1.0
|
N
|
A:TRP203
|
4.8
|
18.3
|
1.0
|
NE1
|
A:TRP203
|
4.8
|
15.7
|
1.0
|
CD1
|
A:PHE202
|
4.9
|
28.5
|
1.0
|
O
|
A:HOH565
|
4.9
|
25.7
|
1.0
|
O
|
A:ASP200
|
5.0
|
22.1
|
1.0
|
|
Calcium binding site 3 out
of 3 in 5lab
Go back to
Calcium Binding Sites List in 5lab
Calcium binding site 3 out
of 3 in the Crystal Structure of the Catalytic Domain of Human MMP12 Complexed with the Inhibitor Nngh
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 the Catalytic Domain of Human MMP12 Complexed with the Inhibitor Nngh within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca305
b:16.0
occ:1.00
|
O
|
A:GLY176
|
2.3
|
18.4
|
1.0
|
O
|
A:GLY178
|
2.3
|
19.6
|
1.0
|
O
|
A:ILE180
|
2.3
|
15.5
|
1.0
|
OE2
|
A:GLU201
|
2.3
|
20.8
|
1.0
|
OD1
|
A:ASP198
|
2.3
|
15.5
|
1.0
|
OD2
|
A:ASP175
|
2.3
|
17.0
|
1.0
|
CG
|
A:ASP198
|
3.4
|
15.9
|
1.0
|
C
|
A:ILE180
|
3.4
|
13.9
|
1.0
|
C
|
A:GLY178
|
3.5
|
20.3
|
1.0
|
CG
|
A:ASP175
|
3.5
|
18.5
|
1.0
|
C
|
A:GLY176
|
3.5
|
17.2
|
1.0
|
CD
|
A:GLU201
|
3.5
|
19.8
|
1.0
|
N
|
A:ILE180
|
3.9
|
16.0
|
1.0
|
N
|
A:GLY178
|
3.9
|
19.8
|
1.0
|
CB
|
A:ASP198
|
4.0
|
13.8
|
1.0
|
N
|
A:GLY176
|
4.1
|
17.8
|
1.0
|
OD1
|
A:ASP175
|
4.1
|
17.0
|
1.0
|
OE1
|
A:GLU201
|
4.1
|
21.4
|
1.0
|
CA
|
A:ILE180
|
4.2
|
14.7
|
1.0
|
C
|
A:LYS177
|
4.2
|
23.2
|
1.0
|
C
|
A:ASP175
|
4.2
|
18.5
|
1.0
|
C
|
A:GLY179
|
4.2
|
17.9
|
1.0
|
N
|
A:ASP175
|
4.3
|
17.8
|
1.0
|
CA
|
A:GLY178
|
4.3
|
22.4
|
1.0
|
OD2
|
A:ASP198
|
4.4
|
16.4
|
1.0
|
CA
|
A:GLY176
|
4.4
|
18.3
|
1.0
|
N
|
A:LEU181
|
4.4
|
13.1
|
1.0
|
N
|
A:LYS177
|
4.5
|
20.5
|
1.0
|
CA
|
A:LYS177
|
4.5
|
22.4
|
1.0
|
N
|
A:GLY179
|
4.5
|
20.8
|
1.0
|
CA
|
A:LEU181
|
4.6
|
14.2
|
1.0
|
CA
|
A:ASP175
|
4.6
|
17.5
|
1.0
|
CA
|
A:GLY179
|
4.6
|
20.2
|
1.0
|
CG
|
A:GLU201
|
4.6
|
18.9
|
1.0
|
CB
|
A:ASP175
|
4.7
|
18.6
|
1.0
|
O
|
A:ASP175
|
4.7
|
19.8
|
1.0
|
CB
|
A:ILE180
|
4.7
|
14.4
|
1.0
|
O
|
A:LYS177
|
4.7
|
24.5
|
1.0
|
O
|
A:GLY179
|
4.8
|
19.6
|
1.0
|
|
Reference:
L.Benda,
J.Mares,
E.Ravera,
G.Parigi,
C.Luchinat,
M.Kaupp,
J.Vaara.
First-Principles Calculation of Pseudo-Contact Shifts in A Paramagnetic Metalloprotein To Be Published.
Page generated: Mon Jul 15 07:29:02 2024
|