Manganese in PDB 6quf: Protein Crystallization By Ionic Liquid Hydrogel Support: Reference Crystal of Glucose Isomerase Grown on Standard Silanized Glass
Enzymatic activity of Protein Crystallization By Ionic Liquid Hydrogel Support: Reference Crystal of Glucose Isomerase Grown on Standard Silanized Glass
All present enzymatic activity of Protein Crystallization By Ionic Liquid Hydrogel Support: Reference Crystal of Glucose Isomerase Grown on Standard Silanized Glass:
5.3.1.5;
Protein crystallography data
The structure of Protein Crystallization By Ionic Liquid Hydrogel Support: Reference Crystal of Glucose Isomerase Grown on Standard Silanized Glass, PDB code: 6quf
was solved by
B.D.Belviso,
R.Caliandro,
R.Caliandro,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
39.93 /
1.19
|
Space group
|
I 2 2 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
92.522,
98.167,
101.851,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
10.7 /
12.9
|
Manganese Binding Sites:
The binding sites of Manganese atom in the Protein Crystallization By Ionic Liquid Hydrogel Support: Reference Crystal of Glucose Isomerase Grown on Standard Silanized Glass
(pdb code 6quf). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the
Protein Crystallization By Ionic Liquid Hydrogel Support: Reference Crystal of Glucose Isomerase Grown on Standard Silanized Glass, PDB code: 6quf:
Jump to Manganese binding site number:
1;
2;
Manganese binding site 1 out
of 2 in 6quf
Go back to
Manganese Binding Sites List in 6quf
Manganese binding site 1 out
of 2 in the Protein Crystallization By Ionic Liquid Hydrogel Support: Reference Crystal of Glucose Isomerase Grown on Standard Silanized Glass
 Mono view
 Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Protein Crystallization By Ionic Liquid Hydrogel Support: Reference Crystal of Glucose Isomerase Grown on Standard Silanized Glass within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn401
b:9.6
occ:0.47
|
OE1
|
A:GLU217
|
2.0
|
12.9
|
1.0
|
HE2
|
A:HIS220
|
2.0
|
12.4
|
0.0
|
O
|
A:HOH798
|
2.2
|
15.2
|
0.9
|
OD2
|
A:ASP255
|
2.2
|
21.1
|
1.0
|
OD1
|
A:ASP255
|
2.3
|
18.7
|
1.0
|
OD1
|
A:ASP257
|
2.3
|
15.0
|
1.0
|
CG
|
A:ASP255
|
2.5
|
16.8
|
1.0
|
NE2
|
A:HIS220
|
2.7
|
12.4
|
1.0
|
CD
|
A:GLU217
|
3.0
|
8.9
|
1.0
|
HD2
|
A:HIS220
|
3.1
|
8.8
|
1.0
|
CD2
|
A:HIS220
|
3.2
|
8.8
|
1.0
|
HD21
|
A:ASN247
|
3.3
|
7.4
|
0.0
|
CG
|
A:ASP257
|
3.3
|
12.6
|
1.0
|
OE2
|
A:GLU217
|
3.5
|
17.2
|
1.0
|
OD2
|
A:ASP257
|
3.5
|
20.0
|
1.0
|
O
|
A:HOH778
|
3.6
|
25.8
|
1.0
|
CE1
|
A:HIS220
|
3.8
|
15.3
|
1.0
|
HD22
|
A:ASN247
|
3.8
|
7.4
|
0.0
|
ND2
|
A:ASN247
|
3.9
|
7.4
|
1.0
|
HO1
|
A:GOL404
|
4.0
|
15.4
|
0.0
|
HE3
|
A:LYS183
|
4.0
|
9.0
|
1.0
|
CB
|
A:ASP255
|
4.0
|
12.4
|
1.0
|
HE1
|
A:HIS220
|
4.2
|
11.6
|
1.0
|
O
|
A:HOH605
|
4.2
|
10.9
|
1.0
|
HZ1
|
A:LYS183
|
4.3
|
13.5
|
1.0
|
HG2
|
A:GLU217
|
4.3
|
6.8
|
1.0
|
CG
|
A:GLU217
|
4.3
|
6.8
|
1.0
|
HB2
|
A:ASP255
|
4.3
|
10.4
|
1.0
|
O1
|
A:GOL404
|
4.4
|
15.4
|
0.9
|
CG
|
A:HIS220
|
4.4
|
7.7
|
1.0
|
HB3
|
A:ASP255
|
4.5
|
12.0
|
1.0
|
HA
|
A:ASP257
|
4.6
|
7.6
|
1.0
|
OD2
|
A:ASP287
|
4.6
|
12.0
|
1.0
|
HZ2
|
A:LYS183
|
4.6
|
12.4
|
1.0
|
CB
|
A:ASP257
|
4.6
|
9.5
|
1.0
|
O
|
A:HOH536
|
4.7
|
34.4
|
0.8
|
H
|
A:ASP257
|
4.7
|
6.3
|
1.0
|
ND1
|
A:HIS220
|
4.7
|
9.9
|
1.0
|
NZ
|
A:LYS183
|
4.8
|
14.2
|
1.0
|
CE
|
A:LYS183
|
4.8
|
8.7
|
1.0
|
MN
|
A:MN402
|
4.9
|
7.9
|
0.5
|
HA3
|
A:GLY219
|
4.9
|
5.4
|
1.0
|
HG3
|
A:GLU217
|
4.9
|
6.9
|
1.0
|
HA
|
A:ASP255
|
4.9
|
8.6
|
1.0
|
CA
|
A:ASP255
|
5.0
|
8.1
|
1.0
|
HZ3
|
A:LYS289
|
5.0
|
13.2
|
0.5
|
CA
|
A:ASP257
|
5.0
|
7.3
|
1.0
|
|
Manganese binding site 2 out
of 2 in 6quf
Go back to
Manganese Binding Sites List in 6quf
Manganese binding site 2 out
of 2 in the Protein Crystallization By Ionic Liquid Hydrogel Support: Reference Crystal of Glucose Isomerase Grown on Standard Silanized Glass
 Mono view
 Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Protein Crystallization By Ionic Liquid Hydrogel Support: Reference Crystal of Glucose Isomerase Grown on Standard Silanized Glass within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn402
b:7.9
occ:0.54
|
OE2
|
A:GLU217
|
2.0
|
17.2
|
1.0
|
OD2
|
A:ASP287
|
2.0
|
12.0
|
1.0
|
OE2
|
A:GLU181
|
2.1
|
13.2
|
1.0
|
O2
|
A:GOL404
|
2.2
|
12.8
|
0.9
|
OD2
|
A:ASP245
|
2.2
|
11.3
|
1.0
|
O1
|
A:GOL404
|
2.2
|
15.4
|
0.9
|
HO2
|
A:GOL404
|
2.8
|
12.7
|
0.0
|
HO1
|
A:GOL404
|
2.8
|
15.4
|
0.0
|
CD
|
A:GLU181
|
3.0
|
11.9
|
1.0
|
C1
|
A:GOL404
|
3.1
|
16.6
|
0.9
|
CG
|
A:ASP287
|
3.1
|
7.9
|
1.0
|
C2
|
A:GOL404
|
3.1
|
13.8
|
0.9
|
CD
|
A:GLU217
|
3.2
|
8.9
|
1.0
|
OE1
|
A:GLU181
|
3.3
|
10.6
|
1.0
|
H12
|
A:GOL404
|
3.3
|
16.4
|
0.9
|
CG
|
A:ASP245
|
3.4
|
8.9
|
1.0
|
HB3
|
A:ASP287
|
3.4
|
6.8
|
1.0
|
HB2
|
A:GLU217
|
3.5
|
6.0
|
1.0
|
H2
|
A:GOL404
|
3.5
|
12.5
|
0.9
|
HB2
|
A:ASP287
|
3.5
|
6.8
|
1.0
|
HE1
|
A:HIS220
|
3.6
|
11.6
|
1.0
|
CB
|
A:ASP287
|
3.6
|
6.6
|
1.0
|
HB3
|
A:ASP245
|
3.7
|
7.2
|
1.0
|
O
|
A:HOH798
|
3.9
|
15.2
|
0.9
|
H11
|
A:GOL404
|
4.0
|
15.6
|
0.9
|
CB
|
A:ASP245
|
4.0
|
7.2
|
1.0
|
HB2
|
A:ASP245
|
4.0
|
7.2
|
1.0
|
O
|
A:HOH698
|
4.0
|
13.7
|
0.9
|
CE1
|
A:HIS220
|
4.0
|
15.3
|
1.0
|
OE1
|
A:GLU217
|
4.1
|
12.9
|
1.0
|
CG
|
A:GLU217
|
4.1
|
6.8
|
1.0
|
CB
|
A:GLU217
|
4.2
|
5.8
|
1.0
|
OD1
|
A:ASP287
|
4.2
|
8.2
|
1.0
|
HG3
|
A:GLU217
|
4.3
|
6.9
|
1.0
|
OD1
|
A:ASP245
|
4.4
|
9.8
|
1.0
|
CG
|
A:GLU181
|
4.4
|
8.4
|
1.0
|
C3
|
A:GOL404
|
4.4
|
10.1
|
0.9
|
HE2
|
A:HIS220
|
4.5
|
12.4
|
0.0
|
HB3
|
A:GLU217
|
4.5
|
6.0
|
1.0
|
H31
|
A:GOL404
|
4.5
|
10.4
|
0.9
|
HD21
|
A:ASN215
|
4.5
|
9.6
|
0.0
|
NE2
|
A:HIS220
|
4.5
|
12.4
|
1.0
|
HG2
|
A:GLU181
|
4.6
|
8.7
|
1.0
|
HZ2
|
A:TRP16
|
4.6
|
7.3
|
1.0
|
HG3
|
A:GLU181
|
4.6
|
8.7
|
1.0
|
HD22
|
A:ASN215
|
4.7
|
9.6
|
0.0
|
H32
|
A:GOL404
|
4.8
|
10.2
|
0.9
|
ND1
|
A:HIS220
|
4.8
|
9.9
|
1.0
|
MN
|
A:MN401
|
4.9
|
9.6
|
0.5
|
ND2
|
A:ASN215
|
4.9
|
9.6
|
1.0
|
|
Reference:
B.D.Belviso,
R.Caliandro,
S.M.Salehi,
G.Di Profio,
R.Caliandro.
Protein Crystallization in Ionic-Liquid Hydrogel Composite Membranes Crystals 2019.
ISSN: ESSN 2073-4352
DOI: 10.3390/CRYST9050253
Page generated: Sun Oct 6 06:08:14 2024
|