Calcium in PDB 2poj: uc(Nmr) Solution Structure of the Inhibitor-Free State of Macrophage Metalloelastase (Mmp-12)

All present enzymatic activity of uc(Nmr) Solution Structure of the Inhibitor-Free State of Macrophage Metalloelastase (Mmp-12):
3.4.24.65;

The structure of uc(Nmr) Solution Structure of the Inhibitor-Free State of Macrophage Metalloelastase (Mmp-12) also contains other interesting chemical elements:

Zinc

(Zn)

40 atoms

The binding sites of Calcium atom in the uc(Nmr) Solution Structure of the Inhibitor-Free State of Macrophage Metalloelastase (Mmp-12) (pdb code 2poj). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the uc(Nmr) Solution Structure of the Inhibitor-Free State of Macrophage Metalloelastase (Mmp-12), PDB code: 2poj:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the uc(Nmr) Solution Structure of the Inhibitor-Free State of Macrophage Metalloelastase (Mmp-12)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of uc(Nmr) Solution Structure of the Inhibitor-Free State of Macrophage Metalloelastase (Mmp-12) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca266 b:0.4 occ:1.00 OE2 A:GLU201 2.5 74.2 1.0 O A:GLY176 2.5 12.5 1.0 O A:ILE180 2.5 25.2 1.0 O A:GLY178 2.6 41.2 1.0 OD1 A:ASP175 2.6 11.1 1.0 OD2 A:ASP198 2.6 64.1 1.0 C A:ILE180 3.1 60.5 1.0 C A:GLY178 3.3 61.3 1.0 CD A:GLU201 3.3 40.1 1.0 CG A:ASP198 3.4 25.3 1.0 C A:GLY179 3.4 73.3 1.0 HA A:LEU181 3.4 22.2 1.0 HB3 A:ASP198 3.5 51.2 1.0 N A:ILE180 3.5 10.0 1.0 HB2 A:ASP198 3.5 74.5 1.0 C A:GLY176 3.6 20.4 1.0 O A:GLY179 3.6 41.4 1.0 CG A:ASP175 3.7 51.4 1.0 HG2 A:GLU201 3.7 53.5 1.0 CB A:ASP198 3.7 5.2 1.0 H A:ILE180 3.8 60.0 1.0 H A:ASP175 3.8 73.2 1.0 CA A:ILE180 3.8 41.1 1.0 HG3 A:GLU201 3.9 4.2 1.0 CG A:GLU201 3.9 52.1 1.0 N A:LEU181 3.9 23.5 1.0 HA3 A:GLY179 3.9 71.4 1.0 N A:GLY179 3.9 22.2 1.0 HB A:ILE180 3.9 31.2 1.0 HD22 A:LEU181 3.9 45.3 1.0 CA A:GLY179 4.0 74.3 1.0 N A:GLY178 4.0 75.3 1.0 OE1 A:GLU201 4.1 52.3 1.0 CA A:GLY178 4.1 43.5 1.0 N A:GLY176 4.2 20.0 1.0 CA A:LEU181 4.2 41.2 1.0 C A:LYS177 4.2 50.4 1.0 H A:GLY178 4.2 62.4 1.0 OD2 A:ASP175 4.2 61.4 1.0 HD11 A:LEU181 4.3 0.2 1.0 C A:ASP175 4.3 31.0 1.0 H A:GLY176 4.3 52.3 1.0 CA A:GLY176 4.4 44.3 1.0 OD1 A:ASP198 4.4 73.3 1.0 O A:LYS177 4.4 33.2 1.0 HA2 A:GLY178 4.5 40.4 1.0 CB A:ILE180 4.5 31.1 1.0 HA2 A:GLY176 4.5 24.5 1.0 HB3 A:PHE174 4.6 41.1 1.0 O A:ASP175 4.6 54.5 1.0 N A:LYS177 4.6 52.2 1.0 H A:LEU181 4.6 0.2 1.0 N A:ASP175 4.6 23.2 1.0 HA A:LYS177 4.7 53.5 1.0 H A:GLY179 4.7 71.3 1.0 CA A:LYS177 4.8 44.1 1.0 HB2 A:ASP200 4.8 65.0 1.0 HA A:ILE180 4.8 54.2 1.0 CB A:ASP175 4.8 12.4 1.0 CA A:ASP175 4.8 23.5 1.0 HD1 A:PHE174 4.9 33.5 1.0 C A:LEU181 4.9 24.1 1.0 CD2 A:LEU181 4.9 2.0 1.0 HG13 A:ILE180 4.9 5.0 1.0

Calcium binding site 2 out of 3 in the uc(Nmr) Solution Structure of the Inhibitor-Free State of Macrophage Metalloelastase (Mmp-12)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of uc(Nmr) Solution Structure of the Inhibitor-Free State of Macrophage Metalloelastase (Mmp-12) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca267 b:73.0 occ:1.00 O A:GLY192 2.5 10.4 1.0 O A:ASP158 2.6 64.3 1.0 O A:GLY190 2.6 44.2 1.0 OD1 A:ASP194 2.6 21.4 1.0 HA A:ILE191 2.9 25.2 1.0 HB2 A:LEU160 3.0 34.3 1.0 O A:ALA157 3.2 61.5 1.0 N A:GLY192 3.2 72.2 1.0 H A:GLY192 3.2 42.3 1.0 HA A:ASP158 3.2 72.2 1.0 C A:ILE191 3.2 33.2 1.0 C A:GLY190 3.3 42.1 1.0 C A:ASP158 3.4 44.5 1.0 CA A:ILE191 3.4 2.1 1.0 C A:GLY192 3.5 72.4 1.0 H A:LEU160 3.6 41.2 1.0 N A:ILE191 3.6 63.2 1.0 CA A:ASP158 3.8 14.2 1.0 CG A:ASP194 3.8 13.4 1.0 O A:ILE191 3.8 73.3 1.0 CA A:GLY192 3.9 30.4 1.0 HD22 A:LEU160 3.9 3.5 1.0 C A:ALA157 4.1 1.0 1.0 CB A:LEU160 4.1 34.4 1.0 N A:LEU160 4.2 72.2 1.0 HA A:ASP194 4.3 21.3 1.0 CA A:GLY190 4.4 24.2 1.0 HA3 A:GLY192 4.4 54.4 1.0 N A:ASP158 4.4 11.1 1.0 H A:ILE191 4.4 71.2 1.0 HD12 A:LEU160 4.4 52.1 1.0 N A:ILE159 4.5 12.4 1.0 H A:ASP194 4.5 23.2 1.0 HB3 A:LEU160 4.5 52.0 1.0 OD2 A:ASP194 4.5 53.0 1.0 N A:ASP194 4.5 71.0 1.0 HA2 A:GLY190 4.5 11.1 1.0 HA A:ILE159 4.6 23.1 1.0 N A:GLY190 4.7 22.4 1.0 N A:GLY193 4.7 2.2 1.0 CA A:LEU160 4.8 21.2 1.0 HA2 A:GLY192 4.8 14.5 1.0 CA A:ASP194 4.8 73.2 1.0 CB A:ILE191 4.9 45.4 1.0 CD2 A:LEU160 4.9 33.4 1.0 C A:GLY193 4.9 40.3 1.0 CB A:ASP194 4.9 24.1 1.0 CG A:LEU160 4.9 51.5 1.0 C A:ILE159 4.9 12.2 1.0 CA A:ILE159 4.9 60.1 1.0 H A:GLY190 4.9 5.2 1.0 OD1 A:ASP158 5.0 75.3 1.0 HD11 A:LEU160 5.0 3.4 1.0

Calcium binding site 3 out of 3 in the uc(Nmr) Solution Structure of the Inhibitor-Free State of Macrophage Metalloelastase (Mmp-12)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of uc(Nmr) Solution Structure of the Inhibitor-Free State of Macrophage Metalloelastase (Mmp-12) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca268 b:3.2 occ:1.00 O A:GLU199 2.6 42.4 1.0 OE2 A:GLU199 2.6 11.2 1.0 OD2 A:ASP124 2.7 24.3 1.0 O A:GLU201 2.7 51.4 1.0 OD1 A:ASP124 2.8 10.4 1.0 CG A:ASP124 3.0 65.0 1.0 HA A:PHE202 3.5 31.1 1.0 O A:ASP200 3.6 1.5 1.0 C A:GLU201 3.6 30.3 1.0 C A:ASP200 3.7 30.4 1.0 C A:GLU199 3.7 75.3 1.0 HA A:ASP200 3.8 51.3 1.0 CD A:GLU199 3.8 34.4 1.0 N A:GLU201 4.1 51.2 1.0 CA A:ASP200 4.2 21.5 1.0 N A:PHE202 4.4 21.1 1.0 HG1 A:THR122 4.4 14.2 1.0 HG2 A:GLU199 4.4 34.2 1.0 CB A:ASP124 4.4 11.0 1.0 N A:ASP200 4.4 31.1 1.0 CA A:PHE202 4.4 74.4 1.0 CA A:GLU201 4.5 3.1 1.0 HB3 A:ASP124 4.5 33.5 1.0 OE1 A:GLU199 4.5 54.2 1.0 H A:GLU201 4.6 22.4 1.0 H A:TRP203 4.6 53.4 1.0 CG A:GLU199 4.7 15.2 1.0 HD1 A:TRP203 4.7 70.4 1.0 HG2 A:PRO123 4.7 30.5 1.0 HA A:GLU199 4.8 33.3 1.0 CA A:GLU199 4.9 0.4 1.0 HB2 A:ASP124 4.9 54.2 1.0 HA A:GLU201 4.9 32.2 1.0 OG1 A:THR122 4.9 74.1 1.0

R.Bhaskaran, M.O.Palmier, N.A.Bagegni, X.Liang, S.R.Van Doren. Solution Structure of Inhibitor-Free Human Metalloelastase (Mmp-12) Indicates An Internal Conformational Adjustment. J.Mol.Biol. V. 374 1333 2007.
ISSN: ISSN 0022-2836
PubMed: 17997411
DOI: 10.1016/J.JMB.2007.10.028