Zinc in PDB 5ue5: Prommp-7 with Heparin Octasaccharide Bound to the Catalytic Domain
Enzymatic activity of Prommp-7 with Heparin Octasaccharide Bound to the Catalytic Domain
All present enzymatic activity of Prommp-7 with Heparin Octasaccharide Bound to the Catalytic Domain:
3.4.24.23;
Other elements in 5ue5:
The structure of Prommp-7 with Heparin Octasaccharide Bound to the Catalytic Domain also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Prommp-7 with Heparin Octasaccharide Bound to the Catalytic Domain
(pdb code 5ue5). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the
Prommp-7 with Heparin Octasaccharide Bound to the Catalytic Domain, PDB code: 5ue5:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 5ue5
Go back to
Zinc Binding Sites List in 5ue5
Zinc binding site 1 out
of 2 in the Prommp-7 with Heparin Octasaccharide Bound to the Catalytic Domain
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Prommp-7 with Heparin Octasaccharide Bound to the Catalytic Domain within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn303
b:52.1
occ:1.00
|
NE2
|
A:HIS143
|
2.3
|
62.3
|
1.0
|
OD2
|
A:ASP145
|
2.3
|
0.0
|
1.0
|
NE2
|
A:HIS158
|
2.3
|
3.3
|
1.0
|
ND1
|
A:HIS171
|
2.5
|
43.2
|
1.0
|
HE1
|
A:HIS171
|
2.5
|
4.3
|
1.0
|
CG
|
A:ASP145
|
2.8
|
21.5
|
1.0
|
CE1
|
A:HIS171
|
2.8
|
13.2
|
1.0
|
HZ
|
A:PHE160
|
2.9
|
0.2
|
1.0
|
CD2
|
A:HIS143
|
3.0
|
25.4
|
1.0
|
CE1
|
A:HIS158
|
3.0
|
2.4
|
1.0
|
HD2
|
A:HIS143
|
3.1
|
63.1
|
1.0
|
OD1
|
A:ASP145
|
3.2
|
21.2
|
1.0
|
HE1
|
A:HIS158
|
3.2
|
12.0
|
1.0
|
CD2
|
A:HIS158
|
3.2
|
74.5
|
1.0
|
CE1
|
A:HIS143
|
3.3
|
23.3
|
1.0
|
HB3
|
A:ASP145
|
3.5
|
35.2
|
1.0
|
HD2
|
A:HIS158
|
3.6
|
54.2
|
1.0
|
HE1
|
A:HIS143
|
3.7
|
44.3
|
1.0
|
CB
|
A:ASP145
|
3.7
|
33.0
|
1.0
|
CZ
|
A:PHE160
|
3.9
|
44.5
|
1.0
|
CG
|
A:HIS171
|
3.9
|
4.2
|
1.0
|
NE2
|
A:HIS171
|
4.1
|
3.5
|
1.0
|
ND1
|
A:HIS158
|
4.1
|
2.5
|
1.0
|
CG
|
A:HIS158
|
4.2
|
1.3
|
1.0
|
CG
|
A:HIS143
|
4.2
|
43.3
|
1.0
|
HA2
|
A:GLY141
|
4.2
|
4.4
|
1.0
|
HB2
|
A:ASP145
|
4.3
|
41.3
|
1.0
|
ND1
|
A:HIS143
|
4.3
|
12.3
|
1.0
|
HB2
|
A:HIS171
|
4.5
|
53.4
|
1.0
|
HE2
|
A:PHE160
|
4.6
|
61.2
|
1.0
|
HB3
|
A:HIS171
|
4.6
|
61.3
|
1.0
|
HE1
|
A:PHE160
|
4.6
|
31.1
|
1.0
|
CD2
|
A:HIS171
|
4.6
|
22.2
|
1.0
|
HB1
|
A:ALA139
|
4.6
|
24.4
|
1.0
|
CB
|
A:HIS171
|
4.7
|
62.3
|
1.0
|
CE2
|
A:PHE160
|
4.7
|
74.3
|
1.0
|
CE1
|
A:PHE160
|
4.7
|
43.1
|
1.0
|
HE2
|
A:HIS171
|
4.8
|
4.2
|
1.0
|
H
|
A:GLY144
|
4.9
|
34.0
|
1.0
|
CA
|
A:ASP145
|
5.0
|
14.2
|
1.0
|
HD1
|
A:HIS158
|
5.0
|
30.0
|
1.0
|
|
Zinc binding site 2 out
of 2 in 5ue5
Go back to
Zinc Binding Sites List in 5ue5
Zinc binding site 2 out
of 2 in the Prommp-7 with Heparin Octasaccharide Bound to the Catalytic Domain
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Prommp-7 with Heparin Octasaccharide Bound to the Catalytic Domain within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn304
b:42.1
occ:1.00
|
NE2
|
A:HIS198
|
2.2
|
31.1
|
1.0
|
NE2
|
A:HIS204
|
2.3
|
12.2
|
1.0
|
NE2
|
A:HIS194
|
2.3
|
20.4
|
1.0
|
SG
|
A:CYS67
|
2.5
|
42.5
|
1.0
|
HE1
|
A:HIS204
|
2.6
|
31.4
|
1.0
|
CE1
|
A:HIS204
|
2.7
|
64.5
|
1.0
|
HB3
|
A:CYS67
|
2.8
|
10.5
|
1.0
|
CE1
|
A:HIS198
|
2.9
|
74.2
|
1.0
|
CB
|
A:CYS67
|
3.0
|
71.3
|
1.0
|
HE1
|
A:HIS198
|
3.0
|
4.2
|
1.0
|
HB2
|
A:CYS67
|
3.1
|
41.2
|
1.0
|
CE1
|
A:HIS194
|
3.1
|
24.4
|
1.0
|
CD2
|
A:HIS194
|
3.2
|
51.2
|
1.0
|
HG
|
A:CYS67
|
3.2
|
24.4
|
1.0
|
CD2
|
A:HIS198
|
3.3
|
14.5
|
1.0
|
HE1
|
A:HIS194
|
3.4
|
11.1
|
1.0
|
HG23
|
A:VAL69
|
3.5
|
34.5
|
1.0
|
HD2
|
A:HIS194
|
3.5
|
72.5
|
1.0
|
CD2
|
A:HIS204
|
3.5
|
12.0
|
1.0
|
HD2
|
A:HIS198
|
3.7
|
72.5
|
1.0
|
HB
|
A:VAL69
|
3.7
|
13.3
|
1.0
|
ND1
|
A:HIS204
|
3.8
|
21.2
|
1.0
|
HG21
|
A:VAL69
|
4.0
|
42.4
|
1.0
|
ND1
|
A:HIS198
|
4.0
|
15.1
|
1.0
|
HD2
|
A:HIS204
|
4.1
|
5.4
|
1.0
|
ND1
|
A:HIS194
|
4.1
|
61.4
|
1.0
|
CG2
|
A:VAL69
|
4.1
|
24.1
|
1.0
|
CG
|
A:HIS194
|
4.2
|
24.3
|
1.0
|
CG
|
A:HIS204
|
4.2
|
24.4
|
1.0
|
CG
|
A:HIS198
|
4.2
|
60.3
|
1.0
|
HE1
|
A:MET212
|
4.3
|
41.2
|
1.0
|
H
|
A:VAL69
|
4.4
|
51.4
|
1.0
|
CB
|
A:VAL69
|
4.5
|
12.4
|
1.0
|
HD1
|
A:HIS204
|
4.5
|
33.1
|
1.0
|
NH2
|
A:ARG66
|
4.5
|
11.5
|
1.0
|
CZ
|
A:ARG66
|
4.5
|
24.3
|
1.0
|
CA
|
A:CYS67
|
4.6
|
1.2
|
1.0
|
HH21
|
A:ARG66
|
4.7
|
41.3
|
1.0
|
NE
|
A:ARG66
|
4.7
|
51.0
|
1.0
|
HH22
|
A:ARG66
|
4.8
|
20.2
|
1.0
|
HD2
|
A:ARG66
|
4.8
|
1.0
|
1.0
|
HE
|
A:ARG66
|
4.8
|
20.4
|
1.0
|
HB3
|
A:MET212
|
4.9
|
34.3
|
1.0
|
HG2
|
A:ARG66
|
4.9
|
63.5
|
1.0
|
HD1
|
A:HIS198
|
4.9
|
23.0
|
1.0
|
NH1
|
A:ARG66
|
4.9
|
74.1
|
1.0
|
HA
|
A:CYS67
|
4.9
|
50.3
|
1.0
|
OD2
|
A:ASP71
|
5.0
|
70.1
|
1.0
|
H
|
A:GLY68
|
5.0
|
25.4
|
1.0
|
|
Reference:
Y.G.Fulcher,
S.H.Prior,
S.Masuko,
L.Li,
D.Pu,
F.Zhang,
R.J.Linhardt,
S.R.Van Doren.
Glycan Activation of A Sheddase: Electrostatic Recognition Between Heparin and Prommp-7. Structure V. 25 1100 2017.
ISSN: ISSN 1878-4186
PubMed: 28648610
DOI: 10.1016/J.STR.2017.05.019
Page generated: Mon Oct 28 09:28:35 2024
|