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Calcium in PDB 2mzi: uc(Nmr) Solution Structure of the Pro Form of Human Matrilysin (Prommp-7) in Complex with Anionic Membrane

Enzymatic activity of uc(Nmr) Solution Structure of the Pro Form of Human Matrilysin (Prommp-7) in Complex with Anionic Membrane

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

Other elements in 2mzi:

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

Zinc (Zn) 40 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the uc(Nmr) Solution Structure of the Pro Form of Human Matrilysin (Prommp-7) in Complex with Anionic Membrane (pdb code 2mzi). 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) in Complex with Anionic Membrane, PDB code: 2mzi:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 2mzi

Go back to Calcium Binding Sites List in 2mzi
Calcium binding site 1 out of 2 in the uc(Nmr) Solution Structure of the Pro Form of Human Matrilysin (Prommp-7) in Complex with Anionic Membrane


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) in Complex with Anionic Membrane within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca301

b:0.0
occ:1.00
O A:GLY165 2.4 0.0 1.0
OD1 A:ASP169 2.4 0.0 1.0
OD2 A:ASP169 2.4 0.0 1.0
O A:ASP133 2.4 0.0 1.0
O A:GLY167 2.4 0.0 1.0
CG A:ASP169 2.8 0.0 1.0
C A:GLY167 3.5 0.0 1.0
C A:GLY165 3.5 0.0 1.0
C A:ASP133 3.6 0.0 1.0
N A:GLY167 3.9 0.0 1.0
H A:GLY167 4.0 0.0 1.0
HH2 A:TRP84 4.0 0.0 1.0
HG2 A:MET135 4.0 0.0 1.0
HA A:ASP133 4.0 0.0 1.0
HA A:ILE134 4.1 0.0 1.0
HA2 A:GLY165 4.1 0.0 1.0
H A:MET135 4.1 0.0 1.0
CB A:ASP169 4.3 0.0 1.0
O A:GLY163 4.3 0.0 1.0
H A:ASP169 4.3 0.0 1.0
C A:LEU166 4.3 0.0 1.0
CA A:GLY167 4.3 0.0 1.0
CA A:GLY165 4.4 0.0 1.0
N A:GLY168 4.5 0.0 1.0
CA A:ASP133 4.5 0.0 1.0
N A:LEU166 4.5 0.0 1.0
O A:ALA132 4.5 0.0 1.0
N A:ILE134 4.6 0.0 1.0
HG3 A:MET135 4.6 0.0 1.0
N A:ASP169 4.6 0.0 1.0
O A:LEU166 4.7 0.0 1.0
HZ3 A:TRP84 4.7 0.0 1.0
HA3 A:GLY168 4.7 0.0 1.0
CA A:ILE134 4.7 0.0 1.0
HB2 A:ASP169 4.7 0.0 1.0
HB3 A:ASP169 4.8 0.0 1.0
CG A:MET135 4.8 0.0 1.0
CA A:LEU166 4.8 0.0 1.0
N A:GLY165 4.8 0.0 1.0
HA A:LEU166 4.9 0.0 1.0
CA A:ASP169 4.9 0.0 1.0
N A:MET135 4.9 0.0 1.0
HA A:ASP169 4.9 0.0 1.0
CA A:GLY168 4.9 0.0 1.0
HA2 A:GLY167 5.0 0.0 1.0
CH2 A:TRP84 5.0 0.0 1.0
HB2 A:MET135 5.0 0.0 1.0
H A:GLY163 5.0 0.0 1.0

Calcium binding site 2 out of 2 in 2mzi

Go back to Calcium Binding Sites List in 2mzi
Calcium binding site 2 out of 2 in the uc(Nmr) Solution Structure of the Pro Form of Human Matrilysin (Prommp-7) in Complex with Anionic Membrane


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) in Complex with Anionic Membrane within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca302

b:0.0
occ:1.00
O A:GLY151 2.2 0.0 1.0
OD1 A:ASP150 2.2 0.0 1.0
OE1 A:GLU176 2.3 0.0 1.0
OD2 A:ASP173 2.4 0.0 1.0
O A:THR155 2.4 0.0 1.0
O A:PHE149 2.5 0.0 1.0
O A:GLY153 2.5 0.0 1.0
H A:GLY153 3.2 0.0 1.0
H A:GLY151 3.3 0.0 1.0
C A:GLY151 3.4 0.0 1.0
C A:GLY153 3.4 0.0 1.0
CG A:ASP150 3.5 0.0 1.0
CD A:GLU176 3.6 0.0 1.0
CG A:ASP173 3.6 0.0 1.0
N A:GLY153 3.6 0.0 1.0
C A:THR155 3.6 0.0 1.0
C A:PHE149 3.7 0.0 1.0
HA A:PRO152 3.7 0.0 1.0
HA A:LEU156 3.8 0.0 1.0
HB3 A:PHE149 3.9 0.0 1.0
HB3 A:ASP150 4.0 0.0 1.0
C A:PRO152 4.0 0.0 1.0
N A:GLY151 4.1 0.0 1.0
C A:ASN154 4.1 0.0 1.0
O A:ASN154 4.1 0.0 1.0
CA A:PRO152 4.2 0.0 1.0
HB2 A:GLU176 4.2 0.0 1.0
CA A:GLY153 4.2 0.0 1.0
N A:PRO152 4.2 0.0 1.0
HB3 A:LEU156 4.2 0.0 1.0
CB A:ASP150 4.2 0.0 1.0
OE2 A:GLU176 4.3 0.0 1.0
N A:ASN154 4.3 0.0 1.0
CA A:GLY151 4.3 0.0 1.0
HB2 A:ASP173 4.3 0.0 1.0
N A:THR155 4.4 0.0 1.0
OD2 A:ASP150 4.4 0.0 1.0
OD1 A:ASP173 4.4 0.0 1.0
N A:ASP150 4.4 0.0 1.0
CA A:ASP150 4.5 0.0 1.0
CB A:ASP173 4.5 0.0 1.0
HG23 A:THR155 4.5 0.0 1.0
HB2 A:PHE149 4.5 0.0 1.0
HB3 A:ASP173 4.6 0.0 1.0
CB A:PHE149 4.6 0.0 1.0
CA A:THR155 4.6 0.0 1.0
N A:LEU156 4.6 0.0 1.0
CA A:LEU156 4.6 0.0 1.0
CG A:GLU176 4.6 0.0 1.0
C A:ASP150 4.6 0.0 1.0
CA A:PHE149 4.7 0.0 1.0
CB A:GLU176 4.8 0.0 1.0
HB3 A:PRO65 4.8 0.0 1.0
CA A:ASN154 4.8 0.0 1.0
HA A:PHE149 4.8 0.0 1.0
HG2 A:GLU176 4.8 0.0 1.0
HA A:GLU176 4.8 0.0 1.0
H A:THR155 4.8 0.0 1.0
O A:PRO152 4.9 0.0 1.0
HA3 A:GLY153 4.9 0.0 1.0
HA2 A:GLY151 4.9 0.0 1.0
CB A:LEU156 4.9 0.0 1.0
H A:GLU176 4.9 0.0 1.0

Reference:

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
Page generated: Sat Dec 12 03:47:25 2020

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