Calcium in PDB 2mze: uc(Nmr) Solution Structure of the Pro Form of Human Matrilysin (Prommp-7)

All present enzymatic activity of uc(Nmr) Solution Structure of the Pro Form of Human Matrilysin (Prommp-7):
3.4.24.23;

The structure of uc(Nmr) Solution Structure of the Pro Form of Human Matrilysin (Prommp-7) also contains other interesting chemical elements:

Zinc

(Zn)

40 atoms

The binding sites of Calcium atom in the uc(Nmr) Solution Structure of the Pro Form of Human Matrilysin (Prommp-7) (pdb code 2mze). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the uc(Nmr) Solution Structure of the Pro Form of Human Matrilysin (Prommp-7), PDB code: 2mze:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the uc(Nmr) Solution Structure of the Pro Form of Human Matrilysin (Prommp-7)


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 Pro Form of Human Matrilysin (Prommp-7) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca301 b:52.4 occ:1.00 OD1 A:ASP169 2.4 52.3 1.0 O A:ASP133 2.4 10.4 1.0 O A:GLY165 2.4 74.0 1.0 O A:GLY167 2.4 2.4 1.0 C A:GLY167 3.2 43.4 1.0 O A:LEU166 3.3 65.1 1.0 CG A:ASP169 3.4 21.1 1.0 C A:LEU166 3.4 53.1 1.0 C A:GLY165 3.4 72.2 1.0 C A:ASP133 3.5 30.4 1.0 HA A:ASP133 3.7 75.3 1.0 N A:GLY167 3.8 31.2 1.0 OD2 A:ASP169 3.8 61.1 1.0 C A:GLY168 3.8 32.3 1.0 HA3 A:GLY168 3.8 10.4 1.0 HA A:LEU166 3.9 14.2 1.0 N A:GLY168 4.0 53.0 1.0 N A:ASP169 4.0 42.2 1.0 CA A:LEU166 4.1 60.1 1.0 CA A:GLY167 4.1 2.2 1.0 HA A:ILE134 4.1 53.0 1.0 CA A:GLY168 4.1 74.3 1.0 O A:GLY168 4.1 33.3 1.0 N A:LEU166 4.1 61.4 1.0 CA A:ASP133 4.2 73.0 1.0 H A:ASP169 4.2 51.2 1.0 HA2 A:GLY165 4.2 70.0 1.0 HA A:ASP169 4.2 34.1 1.0 H A:GLY167 4.3 1.5 1.0 HB3 A:ASP133 4.3 31.1 1.0 CA A:GLY165 4.5 11.4 1.0 HA2 A:GLY167 4.5 42.3 1.0 H A:MET135 4.5 31.3 1.0 CA A:ASP169 4.5 63.4 1.0 CB A:ASP169 4.5 34.4 1.0 O A:THR164 4.6 71.4 1.0 N A:ILE134 4.6 15.2 1.0 HH2 A:TRP84 4.6 54.1 1.0 H A:GLY168 4.8 13.1 1.0 CB A:ASP133 4.8 75.4 1.0 CA A:ILE134 4.8 70.5 1.0 HG2 A:MET135 4.9 64.4 1.0 HA3 A:GLY167 5.0 0.4 1.0 O A:ALA132 5.0 22.0 1.0 HG13 A:ILE134 5.0 61.3 1.0

Calcium binding site 2 out of 2 in the uc(Nmr) Solution Structure of the Pro Form of Human Matrilysin (Prommp-7)


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 Pro Form of Human Matrilysin (Prommp-7) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca302 b:13.3 occ:1.00 O A:GLY151 2.2 62.4 1.0 OE2 A:GLU176 2.4 54.2 1.0 O A:THR155 2.4 42.3 1.0 OD2 A:ASP173 2.6 44.2 1.0 OD2 A:ASP150 2.9 0.4 1.0 HG2 A:GLU176 2.9 62.1 1.0 O A:GLY153 3.0 52.5 1.0 O A:ASN154 3.1 22.3 1.0 HA A:PRO152 3.3 3.4 1.0 H A:GLY153 3.3 62.1 1.0 C A:GLY151 3.3 71.4 1.0 CD A:GLU176 3.3 11.4 1.0 N A:GLY153 3.5 50.2 1.0 CG A:GLU176 3.5 21.5 1.0 HB A:THR155 3.6 23.5 1.0 C A:THR155 3.7 44.4 1.0 C A:GLY153 3.7 23.0 1.0 C A:PRO152 3.7 61.4 1.0 CG A:ASP150 3.8 50.2 1.0 CA A:PRO152 3.8 61.3 1.0 HG3 A:GLU176 3.8 20.3 1.0 CG A:ASP173 3.8 63.2 1.0 OD1 A:ASP150 3.9 34.4 1.0 HA A:LEU156 3.9 0.0 1.0 C A:ASN154 4.0 55.1 1.0 N A:PRO152 4.0 31.1 1.0 CA A:GLY153 4.2 70.3 1.0 HB3 A:ASP173 4.4 31.0 1.0 O A:PRO152 4.5 74.3 1.0 HB3 A:ASP175 4.5 12.1 1.0 CA A:THR155 4.5 22.1 1.0 CB A:THR155 4.5 4.2 1.0 CA A:GLY151 4.5 23.2 1.0 OE1 A:GLU176 4.5 10.3 1.0 CB A:ASP173 4.5 34.0 1.0 HB2 A:ASP173 4.5 32.4 1.0 N A:ASN154 4.6 73.2 1.0 N A:THR155 4.6 33.3 1.0 N A:LEU156 4.6 73.5 1.0 N A:GLY151 4.6 53.1 1.0 O A:PHE149 4.7 63.4 1.0 OD1 A:ASP173 4.7 33.4 1.0 CA A:LEU156 4.7 75.0 1.0 HA A:GLU176 4.8 13.0 1.0 H A:GLY151 4.8 53.1 1.0 HA3 A:GLY153 4.9 4.1 1.0 HA2 A:GLY151 4.9 71.2 1.0 CB A:GLU176 4.9 44.3 1.0 HA2 A:GLY153 4.9 24.3 1.0 CA A:ASN154 5.0 1.4 1.0 HG1 A:THR155 5.0 42.2 1.0

S.H.Prior, Y.G.Fulcher, R.K.Koppisetti, A.Jurkevich, S.R.Van Doren. Charge-Triggered Membrane Insertion of Matrix Metalloproteinase-7, Supporter of Innate Immunity and Tumors. Structure V. 23 2099 2015.
ISSN: ISSN 0969-2126
PubMed: 26439767
DOI: 10.1016/J.STR.2015.08.013