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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:

Zinc (Zn) 2 atoms

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

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