Zinc in PDB 2mze: uc(Nmr) Solution Structure of the Pro Form of Human Matrilysin (Prommp-7)
Enzymatic activity of 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;
Other elements in 2mze:
The structure of uc(Nmr) Solution Structure of the Pro Form of Human Matrilysin (Prommp-7) also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc 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 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), PDB code: 2mze:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 2mze
Go back to
Zinc Binding Sites List in 2mze
Zinc 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 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) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn303
b:30.3
occ:1.00
|
NE2
|
A:HIS143
|
2.1
|
61.1
|
1.0
|
OD2
|
A:ASP145
|
2.2
|
70.0
|
1.0
|
NE2
|
A:HIS158
|
2.2
|
72.0
|
1.0
|
HZ
|
A:PHE160
|
2.4
|
51.1
|
1.0
|
ND1
|
A:HIS171
|
2.4
|
15.5
|
1.0
|
HE1
|
A:HIS171
|
2.8
|
1.3
|
1.0
|
CD2
|
A:HIS158
|
2.9
|
24.5
|
1.0
|
CE1
|
A:HIS171
|
2.9
|
72.5
|
1.0
|
CD2
|
A:HIS143
|
3.0
|
61.0
|
1.0
|
HB2
|
A:ASP145
|
3.0
|
22.5
|
1.0
|
HD2
|
A:HIS158
|
3.0
|
61.3
|
1.0
|
CE1
|
A:HIS143
|
3.1
|
51.4
|
1.0
|
CG
|
A:ASP145
|
3.1
|
72.1
|
1.0
|
CE1
|
A:HIS158
|
3.2
|
55.1
|
1.0
|
HD2
|
A:HIS143
|
3.2
|
31.2
|
1.0
|
HE1
|
A:HIS143
|
3.3
|
73.5
|
1.0
|
CZ
|
A:PHE160
|
3.4
|
13.0
|
1.0
|
CB
|
A:ASP145
|
3.4
|
31.2
|
1.0
|
HE1
|
A:HIS158
|
3.6
|
1.1
|
1.0
|
HB3
|
A:ASP145
|
3.6
|
41.3
|
1.0
|
CG
|
A:HIS171
|
3.7
|
32.4
|
1.0
|
HE1
|
A:PHE160
|
3.9
|
21.3
|
1.0
|
CG
|
A:HIS158
|
4.0
|
52.2
|
1.0
|
ND1
|
A:HIS143
|
4.1
|
55.4
|
1.0
|
CG
|
A:HIS143
|
4.1
|
2.3
|
1.0
|
CE1
|
A:PHE160
|
4.1
|
63.2
|
1.0
|
OD1
|
A:ASP145
|
4.1
|
10.5
|
1.0
|
ND1
|
A:HIS158
|
4.1
|
12.2
|
1.0
|
HB3
|
A:HIS171
|
4.2
|
34.4
|
1.0
|
NE2
|
A:HIS171
|
4.2
|
54.3
|
1.0
|
HB2
|
A:HIS171
|
4.2
|
11.4
|
1.0
|
CB
|
A:HIS171
|
4.3
|
23.1
|
1.0
|
CE2
|
A:PHE160
|
4.4
|
62.2
|
1.0
|
HE2
|
A:PHE160
|
4.4
|
1.1
|
1.0
|
CD2
|
A:HIS171
|
4.6
|
13.1
|
1.0
|
CA
|
A:ASP145
|
4.9
|
32.1
|
1.0
|
HE2
|
A:HIS171
|
5.0
|
34.1
|
1.0
|
HD1
|
A:HIS143
|
5.0
|
32.1
|
1.0
|
|
Zinc binding site 2 out
of 2 in 2mze
Go back to
Zinc Binding Sites List in 2mze
Zinc 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 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) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn304
b:33.0
occ:1.00
|
NE2
|
A:HIS194
|
2.1
|
53.2
|
1.0
|
NE2
|
A:HIS204
|
2.1
|
1.4
|
1.0
|
NE2
|
A:HIS198
|
2.1
|
21.5
|
1.0
|
HE1
|
A:HIS198
|
2.4
|
4.4
|
1.0
|
CE1
|
A:HIS198
|
2.5
|
75.2
|
1.0
|
CE1
|
A:HIS204
|
2.6
|
3.5
|
1.0
|
HE1
|
A:HIS204
|
2.6
|
71.4
|
1.0
|
HB2
|
A:CYS67
|
2.9
|
53.2
|
1.0
|
CD2
|
A:HIS194
|
2.9
|
71.4
|
1.0
|
HD2
|
A:HIS194
|
3.0
|
3.3
|
1.0
|
HB3
|
A:CYS67
|
3.0
|
4.3
|
1.0
|
SG
|
A:CYS67
|
3.2
|
55.3
|
1.0
|
CB
|
A:CYS67
|
3.2
|
51.1
|
1.0
|
CE1
|
A:HIS194
|
3.2
|
24.0
|
1.0
|
CD2
|
A:HIS204
|
3.3
|
70.1
|
1.0
|
CD2
|
A:HIS198
|
3.4
|
10.5
|
1.0
|
HG22
|
A:VAL69
|
3.5
|
52.5
|
1.0
|
HE1
|
A:HIS194
|
3.6
|
15.4
|
1.0
|
HD2
|
A:HIS204
|
3.8
|
63.0
|
1.0
|
ND1
|
A:HIS198
|
3.8
|
2.4
|
1.0
|
ND1
|
A:HIS204
|
3.8
|
42.4
|
1.0
|
HD2
|
A:HIS198
|
4.0
|
34.2
|
1.0
|
CG
|
A:HIS194
|
4.1
|
35.3
|
1.0
|
HG
|
A:CYS67
|
4.1
|
65.3
|
1.0
|
CG
|
A:HIS204
|
4.2
|
11.1
|
1.0
|
HE
|
A:ARG66
|
4.2
|
33.1
|
1.0
|
ND1
|
A:HIS194
|
4.2
|
1.1
|
1.0
|
CG
|
A:HIS198
|
4.3
|
3.4
|
1.0
|
HG23
|
A:VAL69
|
4.4
|
54.3
|
1.0
|
CG2
|
A:VAL69
|
4.4
|
22.2
|
1.0
|
NE
|
A:ARG66
|
4.4
|
31.1
|
1.0
|
HG2
|
A:ARG66
|
4.4
|
0.3
|
1.0
|
HB
|
A:VAL69
|
4.4
|
12.2
|
1.0
|
HD2
|
A:ARG66
|
4.5
|
32.2
|
1.0
|
HD1
|
A:HIS198
|
4.5
|
4.4
|
1.0
|
HD1
|
A:HIS204
|
4.6
|
51.2
|
1.0
|
HH21
|
A:ARG66
|
4.6
|
41.3
|
1.0
|
CZ
|
A:ARG66
|
4.7
|
32.0
|
1.0
|
CA
|
A:CYS67
|
4.7
|
40.3
|
1.0
|
H
|
A:VAL69
|
4.7
|
52.4
|
1.0
|
HZ
|
A:PHE45
|
4.8
|
62.4
|
1.0
|
NH2
|
A:ARG66
|
4.8
|
10.4
|
1.0
|
O
|
A:VAL69
|
4.9
|
50.1
|
1.0
|
O
|
A:HIS194
|
4.9
|
61.2
|
1.0
|
CD
|
A:ARG66
|
4.9
|
44.0
|
1.0
|
CB
|
A:VAL69
|
5.0
|
43.2
|
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 02:10:01 2024
|