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:
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: Fri Jul 12 14:23:42 2024
|