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Calcium in PDB 2mls: Membrane Bilayer Complex with Matrix Metalloproteinase-12 at Its Beta- Face

Enzymatic activity of Membrane Bilayer Complex with Matrix Metalloproteinase-12 at Its Beta- Face

All present enzymatic activity of Membrane Bilayer Complex with Matrix Metalloproteinase-12 at Its Beta- Face:
3.4.24.65;

Other elements in 2mls:

The structure of Membrane Bilayer Complex with Matrix Metalloproteinase-12 at Its Beta- Face also contains other interesting chemical elements:

Zinc (Zn) 28 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Membrane Bilayer Complex with Matrix Metalloproteinase-12 at Its Beta- Face (pdb code 2mls). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the Membrane Bilayer Complex with Matrix Metalloproteinase-12 at Its Beta- Face, PDB code: 2mls:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in 2mls

Go back to Calcium Binding Sites List in 2mls
Calcium binding site 1 out of 3 in the Membrane Bilayer Complex with Matrix Metalloproteinase-12 at Its Beta- Face


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Membrane Bilayer Complex with Matrix Metalloproteinase-12 at Its Beta- Face within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca303

b:0.0
occ:1.00
OD2 A:ASP198 2.2 0.0 1.0
OE1 A:GLU201 2.2 0.0 1.0
OD1 A:ASP175 2.3 0.0 1.0
O A:ILE180 2.3 0.0 1.0
O A:GLY178 2.4 0.0 1.0
O A:GLY176 2.5 0.0 1.0
OD2 A:ASP175 2.5 0.0 1.0
CG A:ASP175 2.8 0.0 1.0
CG A:ASP198 3.3 0.0 1.0
C A:GLY178 3.4 0.0 1.0
CD A:GLU201 3.4 0.0 1.0
C A:ILE180 3.5 0.0 1.0
H A:GLY178 3.5 0.0 1.0
H A:GLY176 3.6 0.0 1.0
H A:ILE180 3.6 0.0 1.0
C A:GLY176 3.7 0.0 1.0
HB3 A:ASP198 3.8 0.0 1.0
N A:GLY178 3.8 0.0 1.0
N A:ILE180 3.8 0.0 1.0
HB2 A:ASP198 3.9 0.0 1.0
HD23 A:LEU181 3.9 0.0 1.0
HB2 A:GLU201 3.9 0.0 1.0
H A:ASP175 3.9 0.0 1.0
CB A:ASP198 4.0 0.0 1.0
HB A:ILE180 4.0 0.0 1.0
OE2 A:GLU201 4.0 0.0 1.0
HA A:LYS177 4.1 0.0 1.0
HA A:LEU181 4.1 0.0 1.0
CA A:ILE180 4.2 0.0 1.0
CA A:GLY178 4.2 0.0 1.0
N A:GLY176 4.2 0.0 1.0
C A:GLY179 4.2 0.0 1.0
CB A:ASP175 4.3 0.0 1.0
C A:LYS177 4.3 0.0 1.0
OD1 A:ASP198 4.3 0.0 1.0
N A:GLY179 4.3 0.0 1.0
HA3 A:GLY179 4.5 0.0 1.0
CA A:GLY179 4.5 0.0 1.0
CG A:GLU201 4.5 0.0 1.0
N A:LYS177 4.5 0.0 1.0
N A:LEU181 4.5 0.0 1.0
CA A:LYS177 4.5 0.0 1.0
CB A:GLU201 4.6 0.0 1.0
CA A:GLY176 4.6 0.0 1.0
CB A:ILE180 4.6 0.0 1.0
N A:ASP175 4.6 0.0 1.0
HB3 A:ASP175 4.7 0.0 1.0
HG2 A:GLU201 4.7 0.0 1.0
HA A:GLU201 4.7 0.0 1.0
HA2 A:GLY178 4.8 0.0 1.0
HB2 A:ASP175 4.8 0.0 1.0
N A:GLU201 4.8 0.0 1.0
HB2 A:ASP200 4.8 0.0 1.0
HB3 A:PHE174 4.8 0.0 1.0
CA A:LEU181 4.8 0.0 1.0
CA A:ASP175 4.9 0.0 1.0
H A:GLU201 4.9 0.0 1.0
O A:GLY179 4.9 0.0 1.0
C A:ASP175 4.9 0.0 1.0
CA A:GLU201 5.0 0.0 1.0
CD2 A:LEU181 5.0 0.0 1.0

Calcium binding site 2 out of 3 in 2mls

Go back to Calcium Binding Sites List in 2mls
Calcium binding site 2 out of 3 in the Membrane Bilayer Complex with Matrix Metalloproteinase-12 at Its Beta- Face


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Membrane Bilayer Complex with Matrix Metalloproteinase-12 at Its Beta- Face within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca304

b:0.0
occ:1.00
OD1 A:ASP194 2.2 0.0 1.0
O A:GLY190 2.5 0.0 1.0
O A:ASP158 2.5 0.0 1.0
O A:GLY192 2.5 0.0 1.0
OD2 A:ASP194 2.7 0.0 1.0
CG A:ASP194 2.8 0.0 1.0
H A:GLY192 3.5 0.0 1.0
C A:ASP158 3.6 0.0 1.0
C A:GLY192 3.6 0.0 1.0
C A:GLY190 3.7 0.0 1.0
H A:LEU160 3.8 0.0 1.0
HA3 A:GLY193 3.9 0.0 1.0
HA A:ASP158 4.0 0.0 1.0
HA A:ILE191 4.0 0.0 1.0
HA A:ILE159 4.1 0.0 1.0
H A:GLY190 4.1 0.0 1.0
N A:GLY192 4.2 0.0 1.0
CB A:ASP194 4.3 0.0 1.0
C A:GLY193 4.4 0.0 1.0
N A:GLY193 4.4 0.0 1.0
O A:ALA157 4.4 0.0 1.0
CA A:GLY193 4.4 0.0 1.0
CA A:ASP158 4.4 0.0 1.0
O A:GLY188 4.4 0.0 1.0
HB2 A:LEU160 4.5 0.0 1.0
N A:ASP194 4.5 0.0 1.0
N A:ILE159 4.6 0.0 1.0
N A:GLY190 4.6 0.0 1.0
N A:ILE191 4.6 0.0 1.0
CA A:GLY192 4.6 0.0 1.0
O A:GLY193 4.7 0.0 1.0
HB3 A:ASP194 4.7 0.0 1.0
CA A:ILE191 4.7 0.0 1.0
H A:ASP194 4.7 0.0 1.0
CA A:GLY190 4.7 0.0 1.0
HE3 A:MET156 4.7 0.0 1.0
N A:LEU160 4.7 0.0 1.0
CA A:ILE159 4.8 0.0 1.0
HA A:ASP194 4.8 0.0 1.0
CA A:ASP194 4.8 0.0 1.0
HB2 A:ASP194 4.8 0.0 1.0
C A:ILE191 4.8 0.0 1.0
HB3 A:LEU160 4.9 0.0 1.0
HZ2 A:TRP109 5.0 0.0 1.0
HE1 A:MET156 5.0 0.0 1.0

Calcium binding site 3 out of 3 in 2mls

Go back to Calcium Binding Sites List in 2mls
Calcium binding site 3 out of 3 in the Membrane Bilayer Complex with Matrix Metalloproteinase-12 at Its Beta- Face


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Membrane Bilayer Complex with Matrix Metalloproteinase-12 at Its Beta- Face within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca305

b:0.0
occ:1.00
OE2 A:GLU199 2.2 0.0 1.0
OD1 A:ASP124 2.2 0.0 1.0
OD2 A:ASP124 2.3 0.0 1.0
O A:GLU199 2.4 0.0 1.0
O A:GLU201 2.5 0.0 1.0
CG A:ASP124 2.7 0.0 1.0
CD A:GLU199 3.1 0.0 1.0
HA A:PHE202 3.3 0.0 1.0
HG1 A:THR122 3.5 0.0 1.0
C A:GLU199 3.5 0.0 1.0
HA A:GLU199 3.5 0.0 1.0
OE1 A:GLU199 3.6 0.0 1.0
C A:GLU201 3.7 0.0 1.0
HD1 A:TRP203 3.9 0.0 1.0
H A:TRP203 4.0 0.0 1.0
HD2 A:PRO123 4.0 0.0 1.0
HG2 A:PRO123 4.1 0.0 1.0
HD1 A:PHE202 4.1 0.0 1.0
CA A:GLU199 4.1 0.0 1.0
OG1 A:THR122 4.1 0.0 1.0
CB A:ASP124 4.2 0.0 1.0
CA A:PHE202 4.2 0.0 1.0
HA A:ASP200 4.3 0.0 1.0
CG A:GLU199 4.3 0.0 1.0
N A:PHE202 4.3 0.0 1.0
HG2 A:GLU199 4.4 0.0 1.0
N A:ASP200 4.5 0.0 1.0
HH21 A:ARG165 4.6 0.0 1.0
HB2 A:ASP124 4.6 0.0 1.0
C A:ASP200 4.6 0.0 1.0
N A:GLU201 4.6 0.0 1.0
H A:GLU201 4.7 0.0 1.0
CB A:GLU199 4.7 0.0 1.0
H A:ASP124 4.7 0.0 1.0
CA A:ASP200 4.7 0.0 1.0
HB3 A:ASP124 4.7 0.0 1.0
CD1 A:TRP203 4.8 0.0 1.0
CG A:PRO123 4.8 0.0 1.0
CA A:GLU201 4.8 0.0 1.0
HG3 A:PRO123 4.9 0.0 1.0
N A:TRP203 4.9 0.0 1.0
CD A:PRO123 4.9 0.0 1.0
HB2 A:PHE202 4.9 0.0 1.0

Reference:

R.K.Koppisetti, Y.G.Fulcher, A.Jurkevich, S.H.Prior, J.Xu, M.Lenoir, M.Overduin, S.R.Van Doren. Ambidextrous Binding of Cell and Membrane Bilayers By Soluble Matrix Metalloproteinase-12. Nat Commun V. 5 5552 2014.
ISSN: ESSN 2041-1723
PubMed: 25412686
DOI: 10.1038/NCOMMS6552
Page generated: Sat Dec 12 03:46:55 2020

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