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Zinc 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:

Calcium (Ca) 40 atoms

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total 2 binding sites of Zinc 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 Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2mzi

Go back to Zinc Binding Sites List in 2mzi
Zinc 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 Zinc with other atoms in the Zn 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:Zn303

b:0.0
occ:1.00
OD2 A:ASP145 1.9 0.0 1.0
NE2 A:HIS143 2.1 0.0 1.0
NE2 A:HIS158 2.2 0.0 1.0
ND1 A:HIS171 2.3 0.0 1.0
CE1 A:HIS158 3.0 0.0 1.0
CE1 A:HIS143 3.1 0.0 1.0
CE1 A:HIS171 3.1 0.0 1.0
CG A:ASP145 3.2 0.0 1.0
CD2 A:HIS143 3.2 0.0 1.0
HE1 A:HIS143 3.2 0.0 1.0
HE1 A:HIS171 3.3 0.0 1.0
HE1 A:HIS158 3.3 0.0 1.0
CD2 A:HIS158 3.3 0.0 1.0
HB2 A:HIS171 3.4 0.0 1.0
HD2 A:HIS143 3.4 0.0 1.0
CG A:HIS171 3.5 0.0 1.0
HD2 A:HIS158 3.7 0.0 1.0
HB3 A:HIS171 3.7 0.0 1.0
OD1 A:ASP145 3.8 0.0 1.0
HB2 A:ASP145 3.8 0.0 1.0
CB A:HIS171 3.9 0.0 1.0
CB A:ASP145 4.1 0.0 1.0
ND1 A:HIS158 4.2 0.0 1.0
ND1 A:HIS143 4.3 0.0 1.0
CG A:HIS143 4.3 0.0 1.0
NE2 A:HIS171 4.3 0.0 1.0
CG A:HIS158 4.4 0.0 1.0
HB3 A:ASP145 4.5 0.0 1.0
CD2 A:HIS171 4.5 0.0 1.0
HZ A:PHE149 4.9 0.0 1.0

Zinc binding site 2 out of 2 in 2mzi

Go back to Zinc Binding Sites List in 2mzi
Zinc 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 Zinc with other atoms in the Zn 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:Zn304

b:0.0
occ:1.00
OD1 A:ASP71 2.0 0.0 1.0
OD2 A:ASP71 2.0 0.0 1.0
NE2 A:HIS194 2.4 0.0 1.0
NE2 A:HIS198 2.4 0.0 1.0
CG A:ASP71 2.4 0.0 1.0
NE2 A:HIS204 2.5 0.0 1.0
SG A:CYS67 3.0 0.0 1.0
HE1 A:HIS198 3.2 0.0 1.0
CE1 A:HIS198 3.2 0.0 1.0
CE1 A:HIS194 3.3 0.0 1.0
CD2 A:HIS204 3.4 0.0 1.0
CD2 A:HIS194 3.4 0.0 1.0
CE1 A:HIS204 3.4 0.0 1.0
HD2 A:HIS204 3.5 0.0 1.0
CD2 A:HIS198 3.6 0.0 1.0
HD2 A:HIS194 3.6 0.0 1.0
HE1 A:HIS194 3.6 0.0 1.0
HA A:ASP71 3.7 0.0 1.0
HE1 A:HIS204 3.8 0.0 1.0
HD2 A:HIS198 3.9 0.0 1.0
CB A:ASP71 3.9 0.0 1.0
HG A:CYS67 3.9 0.0 1.0
CA A:ASP71 4.3 0.0 1.0
O A:VAL69 4.4 0.0 1.0
ND1 A:HIS198 4.4 0.0 1.0
HB3 A:CYS67 4.5 0.0 1.0
CG A:HIS204 4.5 0.0 1.0
ND1 A:HIS204 4.5 0.0 1.0
HB3 A:ASP71 4.5 0.0 1.0
ND1 A:HIS194 4.5 0.0 1.0
CB A:CYS67 4.5 0.0 1.0
HB2 A:ASP71 4.5 0.0 1.0
CG A:HIS194 4.6 0.0 1.0
CG A:HIS198 4.6 0.0 1.0
HA A:CYS67 4.8 0.0 1.0
N A:ASP71 4.8 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: Thu Oct 17 02:10:14 2024

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