Manganese in PDB 1pl4: Crystal Structure of Human Mnsod Y166F Mutant
Enzymatic activity of Crystal Structure of Human Mnsod Y166F Mutant
All present enzymatic activity of Crystal Structure of Human Mnsod Y166F Mutant:
1.15.1.1;
Protein crystallography data
The structure of Crystal Structure of Human Mnsod Y166F Mutant, PDB code: 1pl4
was solved by
L.Fan,
J.A.Tainer,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
30.00 /
1.47
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
73.689,
77.711,
135.795,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
20 /
23.7
|
Manganese Binding Sites:
The binding sites of Manganese atom in the Crystal Structure of Human Mnsod Y166F Mutant
(pdb code 1pl4). 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 Human Mnsod Y166F Mutant, PDB code: 1pl4:
Jump to Manganese binding site number:
1;
2;
3;
4;
Manganese binding site 1 out
of 4 in 1pl4
Go back to
Manganese Binding Sites List in 1pl4
Manganese binding site 1 out
of 4 in the Crystal Structure of Human Mnsod Y166F Mutant
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 Human Mnsod Y166F Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn200
b:11.0
occ:1.00
|
O
|
A:HOH201
|
2.0
|
13.0
|
1.0
|
OD2
|
A:ASP159
|
2.1
|
14.4
|
1.0
|
NE2
|
A:HIS163
|
2.2
|
11.1
|
1.0
|
NE2
|
A:HIS26
|
2.2
|
14.6
|
1.0
|
NE2
|
A:HIS74
|
2.2
|
11.6
|
1.0
|
CG
|
A:ASP159
|
3.1
|
14.0
|
1.0
|
CE1
|
A:HIS163
|
3.1
|
15.0
|
1.0
|
CE1
|
A:HIS26
|
3.1
|
11.3
|
1.0
|
CD2
|
A:HIS163
|
3.2
|
8.4
|
1.0
|
CD2
|
A:HIS26
|
3.2
|
15.1
|
1.0
|
CE1
|
A:HIS74
|
3.2
|
9.8
|
1.0
|
CD2
|
A:HIS74
|
3.2
|
11.8
|
1.0
|
OD1
|
A:ASP159
|
3.5
|
12.8
|
1.0
|
CD2
|
A:HIS30
|
4.1
|
23.8
|
1.0
|
CZ2
|
A:TRP123
|
4.2
|
10.8
|
1.0
|
ND1
|
A:HIS163
|
4.2
|
12.8
|
1.0
|
ND1
|
A:HIS26
|
4.3
|
11.8
|
1.0
|
ND1
|
A:HIS74
|
4.3
|
9.0
|
1.0
|
CG
|
A:HIS163
|
4.3
|
8.6
|
1.0
|
CG
|
A:HIS26
|
4.3
|
12.9
|
1.0
|
CG
|
A:HIS74
|
4.4
|
8.8
|
1.0
|
NE2
|
A:GLN143
|
4.4
|
12.6
|
1.0
|
CB
|
A:ASP159
|
4.4
|
12.3
|
1.0
|
NE2
|
A:HIS30
|
4.5
|
23.8
|
1.0
|
CB
|
A:TRP161
|
4.6
|
9.8
|
1.0
|
CG
|
A:TRP161
|
4.6
|
11.2
|
1.0
|
CH2
|
A:TRP123
|
4.8
|
9.8
|
1.0
|
CD1
|
A:TRP161
|
4.8
|
12.1
|
1.0
|
CE2
|
A:TRP123
|
5.0
|
11.9
|
1.0
|
CG
|
A:HIS30
|
5.0
|
27.2
|
1.0
|
|
Manganese binding site 2 out
of 4 in 1pl4
Go back to
Manganese Binding Sites List in 1pl4
Manganese binding site 2 out
of 4 in the Crystal Structure of Human Mnsod Y166F Mutant
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 Human Mnsod Y166F Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn200
b:10.4
occ:1.00
|
OD2
|
B:ASP159
|
2.0
|
13.7
|
1.0
|
O
|
B:HOH202
|
2.1
|
16.7
|
1.0
|
NE2
|
B:HIS74
|
2.1
|
12.2
|
1.0
|
NE2
|
B:HIS26
|
2.2
|
14.7
|
1.0
|
NE2
|
B:HIS163
|
2.2
|
11.5
|
1.0
|
CG
|
B:ASP159
|
3.0
|
14.1
|
1.0
|
CE1
|
B:HIS74
|
3.1
|
12.2
|
1.0
|
CE1
|
B:HIS26
|
3.1
|
10.9
|
1.0
|
CE1
|
B:HIS163
|
3.1
|
13.1
|
1.0
|
CD2
|
B:HIS74
|
3.2
|
11.8
|
1.0
|
CD2
|
B:HIS163
|
3.2
|
11.6
|
1.0
|
CD2
|
B:HIS26
|
3.3
|
11.2
|
1.0
|
OD1
|
B:ASP159
|
3.4
|
16.7
|
1.0
|
ND1
|
B:HIS74
|
4.2
|
13.8
|
1.0
|
CZ2
|
B:TRP123
|
4.2
|
13.8
|
1.0
|
ND1
|
B:HIS26
|
4.2
|
13.9
|
1.0
|
ND1
|
B:HIS163
|
4.3
|
13.6
|
1.0
|
CG
|
B:HIS74
|
4.3
|
10.7
|
1.0
|
CB
|
B:ASP159
|
4.3
|
9.4
|
1.0
|
CG
|
B:HIS26
|
4.3
|
13.6
|
1.0
|
CG
|
B:HIS163
|
4.4
|
13.0
|
1.0
|
CD2
|
B:HIS30
|
4.4
|
27.5
|
1.0
|
NE2
|
B:GLN143
|
4.4
|
9.2
|
1.0
|
CB
|
B:TRP161
|
4.6
|
9.7
|
1.0
|
CG
|
B:TRP161
|
4.6
|
12.5
|
1.0
|
NE2
|
B:HIS30
|
4.8
|
19.9
|
1.0
|
CH2
|
B:TRP123
|
4.8
|
13.2
|
1.0
|
CD1
|
B:TRP161
|
4.8
|
10.4
|
1.0
|
CE2
|
B:TRP123
|
5.0
|
12.5
|
1.0
|
|
Manganese binding site 3 out
of 4 in 1pl4
Go back to
Manganese Binding Sites List in 1pl4
Manganese binding site 3 out
of 4 in the Crystal Structure of Human Mnsod Y166F Mutant
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 Human Mnsod Y166F Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn200
b:10.4
occ:1.00
|
O
|
C:HOH203
|
2.0
|
14.3
|
1.0
|
OD2
|
C:ASP159
|
2.0
|
13.1
|
1.0
|
NE2
|
C:HIS163
|
2.2
|
11.6
|
1.0
|
NE2
|
C:HIS26
|
2.2
|
12.7
|
1.0
|
NE2
|
C:HIS74
|
2.2
|
13.7
|
1.0
|
CG
|
C:ASP159
|
3.1
|
15.8
|
1.0
|
CE1
|
C:HIS26
|
3.1
|
11.0
|
1.0
|
CE1
|
C:HIS74
|
3.2
|
12.2
|
1.0
|
CD2
|
C:HIS163
|
3.2
|
15.6
|
1.0
|
CE1
|
C:HIS163
|
3.2
|
13.4
|
1.0
|
CD2
|
C:HIS74
|
3.2
|
16.2
|
1.0
|
CD2
|
C:HIS26
|
3.2
|
12.3
|
1.0
|
OD1
|
C:ASP159
|
3.5
|
13.0
|
1.0
|
ND1
|
C:HIS26
|
4.2
|
11.7
|
1.0
|
CZ2
|
C:TRP123
|
4.2
|
11.0
|
1.0
|
ND1
|
C:HIS74
|
4.3
|
11.8
|
1.0
|
ND1
|
C:HIS163
|
4.3
|
14.0
|
1.0
|
CG
|
C:HIS26
|
4.3
|
12.3
|
1.0
|
CG
|
C:HIS74
|
4.3
|
13.1
|
1.0
|
CG
|
C:HIS163
|
4.3
|
12.7
|
1.0
|
CB
|
C:ASP159
|
4.4
|
9.6
|
1.0
|
NE2
|
C:GLN143
|
4.4
|
11.3
|
1.0
|
CD2
|
C:HIS30
|
4.5
|
36.8
|
1.0
|
CB
|
C:TRP161
|
4.6
|
9.5
|
1.0
|
CG
|
C:TRP161
|
4.6
|
8.0
|
1.0
|
CD1
|
C:TRP161
|
4.8
|
11.5
|
1.0
|
CH2
|
C:TRP123
|
4.9
|
14.1
|
1.0
|
NE2
|
C:HIS30
|
4.9
|
32.9
|
1.0
|
CE2
|
C:TRP123
|
5.0
|
10.4
|
1.0
|
|
Manganese binding site 4 out
of 4 in 1pl4
Go back to
Manganese Binding Sites List in 1pl4
Manganese binding site 4 out
of 4 in the Crystal Structure of Human Mnsod Y166F Mutant
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 Human Mnsod Y166F Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mn200
b:10.0
occ:1.00
|
O
|
D:HOH204
|
1.9
|
10.6
|
1.0
|
OD2
|
D:ASP159
|
2.0
|
10.0
|
1.0
|
NE2
|
D:HIS74
|
2.1
|
9.1
|
1.0
|
NE2
|
D:HIS26
|
2.2
|
9.1
|
1.0
|
NE2
|
D:HIS163
|
2.2
|
9.9
|
1.0
|
CG
|
D:ASP159
|
3.0
|
9.8
|
1.0
|
CE1
|
D:HIS26
|
3.1
|
12.6
|
1.0
|
CE1
|
D:HIS74
|
3.1
|
9.6
|
1.0
|
CE1
|
D:HIS163
|
3.1
|
7.4
|
1.0
|
CD2
|
D:HIS163
|
3.2
|
11.9
|
1.0
|
CD2
|
D:HIS74
|
3.2
|
9.1
|
1.0
|
CD2
|
D:HIS26
|
3.2
|
9.2
|
1.0
|
OD1
|
D:ASP159
|
3.4
|
12.3
|
1.0
|
CD2
|
D:HIS30
|
4.2
|
21.4
|
1.0
|
ND1
|
D:HIS74
|
4.2
|
11.3
|
1.0
|
ND1
|
D:HIS26
|
4.2
|
11.6
|
1.0
|
ND1
|
D:HIS163
|
4.2
|
9.2
|
1.0
|
CZ2
|
D:TRP123
|
4.2
|
9.8
|
1.0
|
CG
|
D:HIS74
|
4.3
|
7.8
|
1.0
|
CB
|
D:ASP159
|
4.3
|
8.9
|
1.0
|
CG
|
D:HIS26
|
4.3
|
10.4
|
1.0
|
CG
|
D:HIS163
|
4.3
|
10.4
|
1.0
|
NE2
|
D:GLN143
|
4.5
|
12.1
|
1.0
|
NE2
|
D:HIS30
|
4.5
|
14.1
|
1.0
|
CB
|
D:TRP161
|
4.6
|
8.0
|
1.0
|
CG
|
D:TRP161
|
4.7
|
6.4
|
1.0
|
CH2
|
D:TRP123
|
4.8
|
12.4
|
1.0
|
CB
|
D:ALA164
|
4.9
|
11.5
|
1.0
|
CD1
|
D:TRP161
|
4.9
|
11.8
|
1.0
|
CE2
|
D:TRP123
|
5.0
|
11.9
|
1.0
|
|
Reference:
A.S.Hearn,
L.Fan,
J.R.Lepock,
J.P.Luba,
W.B.Greenleaf,
D.E.Cabelli,
J.A.Tainer,
H.S.Nick,
D.N.Silverman.
Amino Acid Substitution at the Dimeric Interface of Human Manganese Superoxide Dismutase J.Biol.Chem. V. 279 5861 2004.
ISSN: ISSN 0021-9258
PubMed: 14638684
DOI: 10.1074/JBC.M311310200
Page generated: Sat Oct 5 12:07:35 2024
|