Zinc in PDB 2oui: D275P Mutant of Alcohol Dehydrogenase From Protozoa Entamoeba Histolytica
Enzymatic activity of D275P Mutant of Alcohol Dehydrogenase From Protozoa Entamoeba Histolytica
All present enzymatic activity of D275P Mutant of Alcohol Dehydrogenase From Protozoa Entamoeba Histolytica:
1.1.1.2;
Protein crystallography data
The structure of D275P Mutant of Alcohol Dehydrogenase From Protozoa Entamoeba Histolytica, PDB code: 2oui
was solved by
F.Frolow,
L.Shimon,
Y.Burstein,
E.Goihberg,
M.Peretz,
O.Dym,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
50.00 /
1.77
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
145.921,
144.104,
80.073,
90.00,
121.44,
90.00
|
R / Rfree (%)
|
14.8 /
17.8
|
Other elements in 2oui:
The structure of D275P Mutant of Alcohol Dehydrogenase From Protozoa Entamoeba Histolytica also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the D275P Mutant of Alcohol Dehydrogenase From Protozoa Entamoeba Histolytica
(pdb code 2oui). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
D275P Mutant of Alcohol Dehydrogenase From Protozoa Entamoeba Histolytica, PDB code: 2oui:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 2oui
Go back to
Zinc Binding Sites List in 2oui
Zinc binding site 1 out
of 4 in the D275P Mutant of Alcohol Dehydrogenase From Protozoa Entamoeba Histolytica
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of D275P Mutant of Alcohol Dehydrogenase From Protozoa Entamoeba Histolytica within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn361
b:19.4
occ:1.00
|
OD2
|
A:ASP150
|
1.9
|
27.1
|
1.0
|
O2
|
A:CAC1001
|
1.9
|
19.1
|
1.0
|
NE2
|
A:HIS59
|
2.1
|
24.1
|
1.0
|
SG
|
A:CYS37
|
2.2
|
26.1
|
1.0
|
CD2
|
A:HIS59
|
3.0
|
22.4
|
1.0
|
CG
|
A:ASP150
|
3.0
|
27.4
|
1.0
|
CB
|
A:CYS37
|
3.1
|
21.1
|
1.0
|
CE1
|
A:HIS59
|
3.1
|
22.5
|
1.0
|
AS
|
A:CAC1001
|
3.2
|
26.5
|
1.0
|
OG
|
A:SER39
|
3.6
|
29.9
|
1.0
|
OD1
|
A:ASP150
|
3.6
|
30.4
|
1.0
|
O1
|
A:CAC1001
|
3.8
|
25.5
|
1.0
|
C2
|
A:CAC1001
|
3.8
|
28.7
|
1.0
|
CB
|
A:SER39
|
3.9
|
24.2
|
1.0
|
CG
|
A:HIS59
|
4.2
|
21.7
|
1.0
|
ND1
|
A:HIS59
|
4.2
|
24.9
|
1.0
|
CB
|
A:ASP150
|
4.2
|
23.0
|
1.0
|
OE2
|
A:GLU60
|
4.3
|
30.2
|
1.0
|
CE
|
A:MET151
|
4.3
|
25.1
|
1.0
|
C2
|
A:EDO2001
|
4.5
|
30.7
|
1.0
|
CA
|
A:CYS37
|
4.5
|
23.8
|
1.0
|
CD
|
A:GLU60
|
4.6
|
27.5
|
1.0
|
C1
|
A:CAC1001
|
4.8
|
26.5
|
1.0
|
N
|
A:SER39
|
4.8
|
23.9
|
1.0
|
C1
|
A:EDO2001
|
5.0
|
33.6
|
1.0
|
|
Zinc binding site 2 out
of 4 in 2oui
Go back to
Zinc Binding Sites List in 2oui
Zinc binding site 2 out
of 4 in the D275P Mutant of Alcohol Dehydrogenase From Protozoa Entamoeba Histolytica
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of D275P Mutant of Alcohol Dehydrogenase From Protozoa Entamoeba Histolytica within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn361
b:19.4
occ:1.00
|
O2
|
B:CAC1001
|
1.8
|
20.4
|
1.0
|
OD2
|
B:ASP150
|
1.9
|
28.4
|
1.0
|
NE2
|
B:HIS59
|
2.0
|
25.2
|
1.0
|
SG
|
B:CYS37
|
2.2
|
25.7
|
1.0
|
CE1
|
B:HIS59
|
3.0
|
24.1
|
1.0
|
CD2
|
B:HIS59
|
3.0
|
22.3
|
1.0
|
CG
|
B:ASP150
|
3.1
|
26.7
|
1.0
|
CB
|
B:CYS37
|
3.1
|
23.7
|
1.0
|
AS
|
B:CAC1001
|
3.2
|
24.4
|
1.0
|
OD1
|
B:ASP150
|
3.7
|
32.2
|
1.0
|
O1
|
B:CAC1001
|
3.7
|
24.5
|
1.0
|
OG
|
B:SER39
|
3.7
|
30.1
|
1.0
|
C2
|
B:CAC1001
|
3.9
|
19.8
|
1.0
|
CB
|
B:SER39
|
4.0
|
24.4
|
1.0
|
ND1
|
B:HIS59
|
4.1
|
23.0
|
1.0
|
CG
|
B:HIS59
|
4.2
|
23.1
|
1.0
|
CB
|
B:ASP150
|
4.3
|
23.0
|
1.0
|
OE2
|
B:GLU60
|
4.3
|
26.3
|
1.0
|
CE
|
B:MET151
|
4.4
|
25.6
|
1.0
|
CA
|
B:CYS37
|
4.6
|
24.1
|
1.0
|
CD
|
B:GLU60
|
4.6
|
25.4
|
1.0
|
C1
|
B:CAC1001
|
4.8
|
29.1
|
1.0
|
N
|
B:SER39
|
4.9
|
23.5
|
1.0
|
|
Zinc binding site 3 out
of 4 in 2oui
Go back to
Zinc Binding Sites List in 2oui
Zinc binding site 3 out
of 4 in the D275P Mutant of Alcohol Dehydrogenase From Protozoa Entamoeba Histolytica
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of D275P Mutant of Alcohol Dehydrogenase From Protozoa Entamoeba Histolytica within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn361
b:18.9
occ:1.00
|
OD2
|
C:ASP150
|
1.9
|
31.0
|
1.0
|
O1
|
C:CAC1001
|
2.0
|
23.9
|
1.0
|
NE2
|
C:HIS59
|
2.0
|
23.2
|
1.0
|
SG
|
C:CYS37
|
2.3
|
25.1
|
1.0
|
CE1
|
C:HIS59
|
3.0
|
24.2
|
1.0
|
CG
|
C:ASP150
|
3.1
|
23.8
|
1.0
|
CD2
|
C:HIS59
|
3.1
|
21.8
|
1.0
|
CB
|
C:CYS37
|
3.1
|
23.8
|
1.0
|
AS
|
C:CAC1001
|
3.2
|
24.5
|
1.0
|
OD1
|
C:ASP150
|
3.6
|
28.3
|
1.0
|
C1
|
C:CAC1001
|
3.7
|
16.9
|
1.0
|
OG
|
C:SER39
|
3.8
|
24.2
|
1.0
|
C2
|
C:CAC1001
|
3.9
|
19.4
|
1.0
|
CB
|
C:SER39
|
3.9
|
24.4
|
1.0
|
ND1
|
C:HIS59
|
4.1
|
21.2
|
1.0
|
CG
|
C:HIS59
|
4.2
|
22.4
|
1.0
|
OE2
|
C:GLU60
|
4.3
|
28.1
|
1.0
|
CB
|
C:ASP150
|
4.3
|
23.3
|
1.0
|
CE
|
C:MET151
|
4.3
|
26.5
|
1.0
|
CA
|
C:CYS37
|
4.6
|
22.9
|
1.0
|
CD
|
C:GLU60
|
4.6
|
25.5
|
1.0
|
O2
|
C:CAC1001
|
4.7
|
29.4
|
1.0
|
N
|
C:SER39
|
4.8
|
24.2
|
1.0
|
CG
|
C:GLU60
|
5.0
|
20.5
|
1.0
|
|
Zinc binding site 4 out
of 4 in 2oui
Go back to
Zinc Binding Sites List in 2oui
Zinc binding site 4 out
of 4 in the D275P Mutant of Alcohol Dehydrogenase From Protozoa Entamoeba Histolytica
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of D275P Mutant of Alcohol Dehydrogenase From Protozoa Entamoeba Histolytica within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn361
b:19.8
occ:1.00
|
O1
|
D:CAC1001
|
2.0
|
22.5
|
1.0
|
OD2
|
D:ASP150
|
2.0
|
29.3
|
1.0
|
NE2
|
D:HIS59
|
2.1
|
21.7
|
1.0
|
SG
|
D:CYS37
|
2.2
|
21.9
|
1.0
|
CD2
|
D:HIS59
|
3.0
|
26.7
|
1.0
|
CE1
|
D:HIS59
|
3.1
|
23.0
|
1.0
|
CB
|
D:CYS37
|
3.1
|
22.2
|
1.0
|
CG
|
D:ASP150
|
3.1
|
29.8
|
1.0
|
AS
|
D:CAC1001
|
3.3
|
25.3
|
1.0
|
OG
|
D:SER39
|
3.6
|
27.3
|
1.0
|
OD1
|
D:ASP150
|
3.7
|
33.6
|
1.0
|
O2
|
D:CAC1001
|
3.8
|
21.6
|
1.0
|
CB
|
D:SER39
|
3.9
|
21.7
|
1.0
|
C1
|
D:CAC1001
|
4.0
|
22.7
|
1.0
|
ND1
|
D:HIS59
|
4.2
|
26.0
|
1.0
|
CG
|
D:HIS59
|
4.2
|
22.5
|
1.0
|
CB
|
D:ASP150
|
4.3
|
23.3
|
1.0
|
OE2
|
D:GLU60
|
4.3
|
26.6
|
1.0
|
CE
|
D:MET151
|
4.5
|
25.2
|
1.0
|
CA
|
D:CYS37
|
4.6
|
22.1
|
1.0
|
CD
|
D:GLU60
|
4.7
|
25.4
|
1.0
|
N
|
D:SER39
|
4.8
|
23.8
|
1.0
|
C2
|
D:CAC1001
|
4.9
|
26.6
|
1.0
|
CA
|
D:SER39
|
5.0
|
23.8
|
1.0
|
|
Reference:
E.Goihberg,
O.Dym,
S.Tel-Or,
L.Shimon,
F.Frolow,
M.Peretz,
Y.Burstein.
Thermal Stabilization of the Protozoan Entamoeba Histolytica Alcohol Dehydrogenase By A Single Proline Substitution. Proteins V. 72 711 2008.
ISSN: ISSN 0887-3585
PubMed: 18260103
DOI: 10.1002/PROT.21946
Page generated: Thu Oct 17 02:46:43 2024
|