Manganese in PDB 1ues: Crystal Structure of Porphyromonas Gingivalis Sod
Enzymatic activity of Crystal Structure of Porphyromonas Gingivalis Sod
All present enzymatic activity of Crystal Structure of Porphyromonas Gingivalis Sod:
1.15.1.1;
Protein crystallography data
The structure of Crystal Structure of Porphyromonas Gingivalis Sod, PDB code: 1ues
was solved by
F.Yamakura,
S.Sugio,
B.Y.Hiraoka,
T.Yokota,
D.Ohmori,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
20.00 /
1.60
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
71.680,
95.120,
98.750,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
22.1 /
25
|
Manganese Binding Sites:
The binding sites of Manganese atom in the Crystal Structure of Porphyromonas Gingivalis Sod
(pdb code 1ues). 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 Porphyromonas Gingivalis Sod, PDB code: 1ues:
Jump to Manganese binding site number:
1;
2;
3;
4;
Manganese binding site 1 out
of 4 in 1ues
Go back to
Manganese Binding Sites List in 1ues
Manganese binding site 1 out
of 4 in the Crystal Structure of Porphyromonas Gingivalis Sod
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 Porphyromonas Gingivalis Sod within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn192
b:18.4
occ:1.00
|
OD2
|
A:ASP157
|
2.1
|
19.7
|
1.0
|
NE2
|
A:HIS27
|
2.2
|
19.6
|
1.0
|
NE2
|
A:HIS74
|
2.2
|
18.9
|
1.0
|
NE2
|
A:HIS161
|
2.2
|
18.5
|
1.0
|
O
|
A:HOH193
|
2.2
|
20.2
|
1.0
|
CD2
|
A:HIS161
|
3.1
|
18.5
|
1.0
|
CE1
|
A:HIS27
|
3.1
|
19.4
|
1.0
|
CG
|
A:ASP157
|
3.1
|
19.9
|
1.0
|
CD2
|
A:HIS74
|
3.2
|
19.5
|
1.0
|
CE1
|
A:HIS74
|
3.2
|
19.3
|
1.0
|
CD2
|
A:HIS27
|
3.2
|
19.9
|
1.0
|
CE1
|
A:HIS161
|
3.3
|
19.0
|
1.0
|
OD1
|
A:ASP157
|
3.6
|
19.6
|
1.0
|
CH2
|
A:TRP123
|
4.1
|
21.4
|
1.0
|
ND1
|
A:HIS27
|
4.2
|
19.6
|
1.0
|
ND1
|
A:HIS74
|
4.3
|
18.9
|
1.0
|
CZ2
|
A:TRP123
|
4.3
|
21.0
|
1.0
|
CG
|
A:HIS74
|
4.3
|
19.3
|
1.0
|
CG
|
A:HIS27
|
4.3
|
20.0
|
1.0
|
CG
|
A:HIS161
|
4.3
|
18.5
|
1.0
|
ND1
|
A:HIS161
|
4.3
|
18.9
|
1.0
|
CB
|
A:ASP157
|
4.4
|
19.3
|
1.0
|
CB
|
A:TRP159
|
4.4
|
19.3
|
1.0
|
CG
|
A:TRP159
|
4.7
|
19.2
|
1.0
|
NE2
|
A:GLN70
|
4.8
|
22.9
|
1.0
|
CB
|
A:ALA162
|
4.8
|
19.4
|
1.0
|
CZ3
|
A:TRP123
|
5.0
|
21.3
|
1.0
|
|
Manganese binding site 2 out
of 4 in 1ues
Go back to
Manganese Binding Sites List in 1ues
Manganese binding site 2 out
of 4 in the Crystal Structure of Porphyromonas Gingivalis Sod
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 Porphyromonas Gingivalis Sod within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn392
b:22.2
occ:1.00
|
O
|
B:HOH393
|
2.1
|
22.3
|
1.0
|
OD2
|
B:ASP357
|
2.1
|
22.7
|
1.0
|
NE2
|
B:HIS361
|
2.2
|
21.6
|
1.0
|
NE2
|
B:HIS227
|
2.2
|
22.4
|
1.0
|
NE2
|
B:HIS274
|
2.2
|
24.2
|
1.0
|
CD2
|
B:HIS361
|
3.1
|
21.9
|
1.0
|
CE1
|
B:HIS227
|
3.1
|
22.1
|
1.0
|
CG
|
B:ASP357
|
3.1
|
23.7
|
1.0
|
CD2
|
B:HIS274
|
3.2
|
24.6
|
1.0
|
CE1
|
B:HIS274
|
3.2
|
24.0
|
1.0
|
CD2
|
B:HIS227
|
3.2
|
22.6
|
1.0
|
CE1
|
B:HIS361
|
3.3
|
22.4
|
1.0
|
OD1
|
B:ASP357
|
3.5
|
23.4
|
1.0
|
CH2
|
B:TRP323
|
4.1
|
25.1
|
1.0
|
CZ2
|
B:TRP323
|
4.2
|
25.2
|
1.0
|
ND1
|
B:HIS227
|
4.2
|
22.7
|
1.0
|
ND1
|
B:HIS274
|
4.3
|
24.7
|
1.0
|
CG
|
B:HIS361
|
4.3
|
22.3
|
1.0
|
CG
|
B:HIS227
|
4.3
|
23.2
|
1.0
|
CG
|
B:HIS274
|
4.3
|
25.0
|
1.0
|
ND1
|
B:HIS361
|
4.3
|
21.9
|
1.0
|
CB
|
B:TRP359
|
4.4
|
20.9
|
1.0
|
CB
|
B:ASP357
|
4.4
|
23.2
|
1.0
|
CG
|
B:TRP359
|
4.7
|
21.2
|
1.0
|
CB
|
B:ALA362
|
4.7
|
21.2
|
1.0
|
NE2
|
B:GLN270
|
4.9
|
28.7
|
1.0
|
|
Manganese binding site 3 out
of 4 in 1ues
Go back to
Manganese Binding Sites List in 1ues
Manganese binding site 3 out
of 4 in the Crystal Structure of Porphyromonas Gingivalis Sod
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 Porphyromonas Gingivalis Sod within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn592
b:21.6
occ:1.00
|
OD2
|
C:ASP557
|
2.1
|
24.3
|
1.0
|
O
|
C:HOH3
|
2.1
|
24.7
|
1.0
|
NE2
|
C:HIS474
|
2.2
|
24.2
|
1.0
|
NE2
|
C:HIS561
|
2.2
|
21.9
|
1.0
|
NE2
|
C:HIS427
|
2.2
|
21.5
|
1.0
|
CE1
|
C:HIS474
|
3.0
|
24.3
|
1.0
|
CD2
|
C:HIS561
|
3.1
|
22.1
|
1.0
|
CE1
|
C:HIS427
|
3.1
|
21.2
|
1.0
|
CG
|
C:ASP557
|
3.1
|
25.1
|
1.0
|
CD2
|
C:HIS427
|
3.2
|
21.5
|
1.0
|
CE1
|
C:HIS561
|
3.2
|
22.4
|
1.0
|
CD2
|
C:HIS474
|
3.2
|
25.2
|
1.0
|
OD1
|
C:ASP557
|
3.5
|
25.0
|
1.0
|
ND1
|
C:HIS474
|
4.2
|
24.9
|
1.0
|
CH2
|
C:TRP523
|
4.2
|
26.3
|
1.0
|
ND1
|
C:HIS427
|
4.2
|
21.5
|
1.0
|
CG
|
C:HIS561
|
4.2
|
22.3
|
1.0
|
ND1
|
C:HIS561
|
4.3
|
22.1
|
1.0
|
CG
|
C:HIS474
|
4.3
|
24.9
|
1.0
|
CG
|
C:HIS427
|
4.3
|
21.4
|
1.0
|
CZ2
|
C:TRP523
|
4.4
|
26.0
|
1.0
|
CB
|
C:ASP557
|
4.4
|
25.3
|
1.0
|
CB
|
C:TRP559
|
4.4
|
22.2
|
1.0
|
CG
|
C:TRP559
|
4.7
|
22.4
|
1.0
|
CB
|
C:ALA562
|
4.9
|
22.8
|
1.0
|
NE2
|
C:GLN470
|
4.9
|
26.6
|
1.0
|
CD1
|
C:TRP559
|
5.0
|
21.9
|
1.0
|
|
Manganese binding site 4 out
of 4 in 1ues
Go back to
Manganese Binding Sites List in 1ues
Manganese binding site 4 out
of 4 in the Crystal Structure of Porphyromonas Gingivalis Sod
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 Porphyromonas Gingivalis Sod within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mn792
b:22.0
occ:1.00
|
OD2
|
D:ASP757
|
2.0
|
22.2
|
1.0
|
NE2
|
D:HIS674
|
2.2
|
21.4
|
1.0
|
NE2
|
D:HIS627
|
2.3
|
23.3
|
1.0
|
O
|
D:HOH4
|
2.3
|
23.1
|
1.0
|
NE2
|
D:HIS761
|
2.3
|
24.6
|
1.0
|
CG
|
D:ASP757
|
3.1
|
22.7
|
1.0
|
CD2
|
D:HIS761
|
3.2
|
23.3
|
1.0
|
CE1
|
D:HIS674
|
3.2
|
22.2
|
1.0
|
CE1
|
D:HIS627
|
3.2
|
23.5
|
1.0
|
CD2
|
D:HIS627
|
3.2
|
24.1
|
1.0
|
CD2
|
D:HIS674
|
3.2
|
22.0
|
1.0
|
CE1
|
D:HIS761
|
3.4
|
23.9
|
1.0
|
OD1
|
D:ASP757
|
3.5
|
22.9
|
1.0
|
CH2
|
D:TRP723
|
4.0
|
23.5
|
1.0
|
CZ2
|
D:TRP723
|
4.1
|
23.5
|
1.0
|
ND1
|
D:HIS627
|
4.3
|
23.9
|
1.0
|
ND1
|
D:HIS674
|
4.3
|
21.9
|
1.0
|
CB
|
D:ASP757
|
4.3
|
22.4
|
1.0
|
CG
|
D:HIS627
|
4.3
|
24.4
|
1.0
|
CG
|
D:HIS674
|
4.3
|
21.9
|
1.0
|
CG
|
D:HIS761
|
4.3
|
23.9
|
1.0
|
ND1
|
D:HIS761
|
4.4
|
24.1
|
1.0
|
CB
|
D:TRP759
|
4.4
|
21.2
|
1.0
|
NE2
|
D:GLN670
|
4.7
|
25.2
|
1.0
|
CG
|
D:TRP759
|
4.7
|
21.3
|
1.0
|
CB
|
D:ALA762
|
4.9
|
21.8
|
1.0
|
CZ3
|
D:TRP723
|
5.0
|
23.7
|
1.0
|
|
Reference:
F.Yamakura,
S.Sugio,
B.Y.Hiraoka,
D.Ohmori,
T.Yokota.
Pronounced Conversion of the Metal-Specific Activity of Superoxide Dismutase From Porphyromonas Gingivalis By the Mutation of A Single Amino Acid (GLY155THR) Located Apart From the Active Site Biochemistry V. 42 10790 2003.
ISSN: ISSN 0006-2960
PubMed: 12962504
DOI: 10.1021/BI0349625
Page generated: Sat Oct 5 12:38:07 2024
|