Manganese in PDB 7w6w: Crystal Structure of A Mutant Staphylococcus Equorum Manganese Superoxide Dismutase L169W
Enzymatic activity of Crystal Structure of A Mutant Staphylococcus Equorum Manganese Superoxide Dismutase L169W
All present enzymatic activity of Crystal Structure of A Mutant Staphylococcus Equorum Manganese Superoxide Dismutase L169W:
1.15.1.1;
Protein crystallography data
The structure of Crystal Structure of A Mutant Staphylococcus Equorum Manganese Superoxide Dismutase L169W, PDB code: 7w6w
was solved by
D.S.Retnoningrum,
H.Yoshida,
A.A.Artarini,
W.T.Ismaya,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
42.59 /
1.94
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
55.245,
136.527,
55.506,
90,
100.91,
90
|
R / Rfree (%)
|
20.2 /
25.6
|
Manganese Binding Sites:
The binding sites of Manganese atom in the Crystal Structure of A Mutant Staphylococcus Equorum Manganese Superoxide Dismutase L169W
(pdb code 7w6w). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the
Crystal Structure of A Mutant Staphylococcus Equorum Manganese Superoxide Dismutase L169W, PDB code: 7w6w:
Jump to Manganese binding site number:
1;
2;
3;
4;
Manganese binding site 1 out
of 4 in 7w6w
Go back to
Manganese Binding Sites List in 7w6w
Manganese binding site 1 out
of 4 in the Crystal Structure of A Mutant Staphylococcus Equorum Manganese Superoxide Dismutase L169W
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Crystal Structure of A Mutant Staphylococcus Equorum Manganese Superoxide Dismutase L169W within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn301
b:25.7
occ:1.00
|
OD2
|
A:ASP161
|
1.8
|
26.1
|
1.0
|
NE2
|
A:HIS27
|
2.0
|
25.8
|
1.0
|
NE2
|
A:HIS165
|
2.1
|
23.1
|
1.0
|
NE2
|
A:HIS81
|
2.1
|
23.5
|
1.0
|
O
|
A:HOH417
|
2.2
|
22.6
|
1.0
|
CG
|
A:ASP161
|
2.9
|
30.2
|
1.0
|
CE1
|
A:HIS27
|
3.0
|
28.0
|
1.0
|
CD2
|
A:HIS27
|
3.1
|
26.7
|
1.0
|
CE1
|
A:HIS81
|
3.1
|
24.8
|
1.0
|
CE1
|
A:HIS165
|
3.1
|
25.0
|
1.0
|
CD2
|
A:HIS165
|
3.1
|
27.6
|
1.0
|
CD2
|
A:HIS81
|
3.2
|
29.9
|
1.0
|
OD1
|
A:ASP161
|
3.4
|
32.1
|
1.0
|
ND1
|
A:HIS27
|
4.1
|
27.6
|
1.0
|
CG
|
A:HIS27
|
4.2
|
26.3
|
1.0
|
ND1
|
A:HIS165
|
4.2
|
26.5
|
1.0
|
ND1
|
A:HIS81
|
4.2
|
26.6
|
1.0
|
CB
|
A:ASP161
|
4.2
|
30.6
|
1.0
|
CG
|
A:HIS165
|
4.3
|
26.4
|
1.0
|
CG
|
A:HIS81
|
4.3
|
28.2
|
1.0
|
CZ2
|
A:TRP128
|
4.5
|
23.5
|
1.0
|
NE2
|
A:GLN146
|
4.6
|
34.7
|
1.0
|
CB
|
A:TRP163
|
4.7
|
28.0
|
1.0
|
CG
|
A:TRP163
|
4.8
|
27.3
|
1.0
|
CB
|
A:ALA166
|
5.0
|
25.7
|
1.0
|
|
Manganese binding site 2 out
of 4 in 7w6w
Go back to
Manganese Binding Sites List in 7w6w
Manganese binding site 2 out
of 4 in the Crystal Structure of A Mutant Staphylococcus Equorum Manganese Superoxide Dismutase L169W
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Crystal Structure of A Mutant Staphylococcus Equorum Manganese Superoxide Dismutase L169W within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn302
b:24.9
occ:1.00
|
OD2
|
B:ASP161
|
2.0
|
24.1
|
1.0
|
NE2
|
B:HIS27
|
2.2
|
27.2
|
1.0
|
NE2
|
B:HIS81
|
2.2
|
23.3
|
1.0
|
O
|
B:HOH447
|
2.3
|
21.5
|
1.0
|
NE2
|
B:HIS165
|
2.3
|
26.6
|
1.0
|
CG
|
B:ASP161
|
3.1
|
21.4
|
1.0
|
CE1
|
B:HIS27
|
3.1
|
25.0
|
1.0
|
CE1
|
B:HIS81
|
3.1
|
23.4
|
1.0
|
CD2
|
B:HIS27
|
3.2
|
27.6
|
1.0
|
CD2
|
B:HIS165
|
3.2
|
24.4
|
1.0
|
CD2
|
B:HIS81
|
3.3
|
24.9
|
1.0
|
CE1
|
B:HIS165
|
3.3
|
30.2
|
1.0
|
OD1
|
B:ASP161
|
3.6
|
23.7
|
1.0
|
ND1
|
B:HIS27
|
4.2
|
26.9
|
1.0
|
CG
|
B:HIS27
|
4.3
|
27.9
|
1.0
|
ND1
|
B:HIS81
|
4.3
|
23.3
|
1.0
|
CB
|
B:ASP161
|
4.3
|
22.2
|
1.0
|
CG
|
B:HIS165
|
4.4
|
27.2
|
1.0
|
CG
|
B:HIS81
|
4.4
|
27.0
|
1.0
|
ND1
|
B:HIS165
|
4.4
|
22.8
|
1.0
|
CZ2
|
B:TRP128
|
4.5
|
24.1
|
1.0
|
NE2
|
B:GLN146
|
4.6
|
17.6
|
1.0
|
CB
|
B:TRP163
|
4.8
|
19.8
|
1.0
|
CG
|
B:TRP163
|
4.8
|
18.9
|
1.0
|
|
Manganese binding site 3 out
of 4 in 7w6w
Go back to
Manganese Binding Sites List in 7w6w
Manganese binding site 3 out
of 4 in the Crystal Structure of A Mutant Staphylococcus Equorum Manganese Superoxide Dismutase L169W
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 3 of Crystal Structure of A Mutant Staphylococcus Equorum Manganese Superoxide Dismutase L169W within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn301
b:26.4
occ:1.00
|
OD2
|
C:ASP161
|
1.9
|
32.1
|
1.0
|
NE2
|
C:HIS81
|
2.1
|
31.8
|
1.0
|
NE2
|
C:HIS165
|
2.1
|
22.9
|
1.0
|
NE2
|
C:HIS27
|
2.1
|
32.0
|
1.0
|
O
|
C:HOH430
|
2.3
|
26.6
|
1.0
|
CG
|
C:ASP161
|
2.9
|
30.8
|
1.0
|
CE1
|
C:HIS81
|
3.0
|
37.5
|
1.0
|
CE1
|
C:HIS165
|
3.1
|
24.4
|
1.0
|
CE1
|
C:HIS27
|
3.1
|
33.5
|
1.0
|
CD2
|
C:HIS81
|
3.1
|
32.0
|
1.0
|
CD2
|
C:HIS27
|
3.1
|
29.2
|
1.0
|
CD2
|
C:HIS165
|
3.1
|
26.1
|
1.0
|
OD1
|
C:ASP161
|
3.4
|
26.8
|
1.0
|
ND1
|
C:HIS81
|
4.1
|
31.2
|
1.0
|
ND1
|
C:HIS165
|
4.2
|
29.1
|
1.0
|
CB
|
C:ASP161
|
4.2
|
29.6
|
1.0
|
CG
|
C:HIS81
|
4.2
|
33.2
|
1.0
|
ND1
|
C:HIS27
|
4.2
|
28.0
|
1.0
|
CG
|
C:HIS27
|
4.3
|
30.3
|
1.0
|
CG
|
C:HIS165
|
4.3
|
27.4
|
1.0
|
CZ2
|
C:TRP128
|
4.5
|
30.6
|
1.0
|
NE2
|
C:GLN146
|
4.7
|
27.3
|
1.0
|
CB
|
C:TRP163
|
4.7
|
24.9
|
1.0
|
CG
|
C:TRP163
|
4.9
|
22.7
|
1.0
|
CB
|
C:ALA166
|
4.9
|
21.8
|
1.0
|
|
Manganese binding site 4 out
of 4 in 7w6w
Go back to
Manganese Binding Sites List in 7w6w
Manganese binding site 4 out
of 4 in the Crystal Structure of A Mutant Staphylococcus Equorum Manganese Superoxide Dismutase L169W
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 4 of Crystal Structure of A Mutant Staphylococcus Equorum Manganese Superoxide Dismutase L169W within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mn302
b:28.2
occ:1.00
|
OD2
|
D:ASP161
|
1.9
|
31.0
|
1.0
|
NE2
|
D:HIS27
|
2.0
|
35.3
|
1.0
|
NE2
|
D:HIS81
|
2.1
|
31.9
|
1.0
|
NE2
|
D:HIS165
|
2.2
|
26.1
|
1.0
|
CE1
|
D:HIS27
|
2.9
|
31.2
|
1.0
|
CG
|
D:ASP161
|
3.0
|
28.0
|
1.0
|
CE1
|
D:HIS81
|
3.1
|
30.4
|
1.0
|
CD2
|
D:HIS81
|
3.1
|
33.9
|
1.0
|
CD2
|
D:HIS27
|
3.1
|
34.2
|
1.0
|
CE1
|
D:HIS165
|
3.1
|
22.3
|
1.0
|
CD2
|
D:HIS165
|
3.2
|
25.5
|
1.0
|
OD1
|
D:ASP161
|
3.4
|
26.1
|
1.0
|
ND1
|
D:HIS27
|
4.1
|
32.0
|
1.0
|
ND1
|
D:HIS81
|
4.2
|
36.8
|
1.0
|
CG
|
D:HIS27
|
4.2
|
30.8
|
1.0
|
CG
|
D:HIS81
|
4.2
|
32.9
|
1.0
|
CB
|
D:ASP161
|
4.2
|
29.5
|
1.0
|
ND1
|
D:HIS165
|
4.3
|
25.7
|
1.0
|
CG
|
D:HIS165
|
4.3
|
25.9
|
1.0
|
CZ2
|
D:TRP128
|
4.5
|
29.1
|
1.0
|
CB
|
D:TRP163
|
4.6
|
25.9
|
1.0
|
NE2
|
D:GLN146
|
4.7
|
27.1
|
1.0
|
CG
|
D:TRP163
|
4.8
|
25.7
|
1.0
|
CB
|
D:ALA166
|
4.9
|
31.0
|
1.0
|
|
Reference:
D.S.Retnoningrum,
H.Yoshida,
A.A.Artarini,
W.T.Ismaya.
Crystal Structure of A Mutant Staphylococcus Equorum Manganese Superoxide Dismutase L169W To Be Published.
Page generated: Sun Oct 6 10:59:13 2024
|